EzCatDB: S00225

DB codeS00225
RLCP classification8.131.42001.6
8.113.42001.5
CATH domainDomain 13.20.20.70Catalytic domain
E.C.5.3.1.1
CSA1hti,1tph
MACiEM0324

CATH domainRelated DB codes (homologues)
3.20.20.70S00215,S00217,S00218,S00219,S00532,S00198,S00220,S00745,S00537,S00538,S00539,S00826,S00841,S00235,S00239,S00240,S00243,S00244,S00199,S00200,S00201,S00221,S00222,S00847,S00224,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,D00863,T00089

Enzyme Name
Swiss-protKEGG

P00943P00940P0A858P62002P62003P48499Q07412P60174P60175P04789P52270P50921P00942
Protein nameTriosephosphate isomeraseTriosephosphate isomeraseTriosephosphate isomeraseTriosephosphate isomeraseTriosephosphate isomeraseTriosephosphate isomeraseTriosephosphate isomeraseTriosephosphate isomeraseTriosephosphate isomeraseTriosephosphate isomerase, glycosomalTriosephosphate isomerase, glycosomalTriosephosphate isomeraseTriosephosphate isomerasetriose-phosphate isomerase
phosphotriose isomerase
triose phosphoisomerase
triose phosphate mutase
D-glyceraldehyde-3-phosphate ketol-isomerase
SynonymsTIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
Triose-phosphate isomerase
EC 5.3.1.1
TIM
Triose-phosphate isomerase
EC 5.3.1.1
TIM
EC 5.3.1.1
Triose-phosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00031Inositol metabolism
MAP00051Fructose and mannose metabolism
MAP00710Carbon fixation in photosynthetic organisms

Swiss-prot:Accession NumberP00943P00940P0A858P62002P62003P48499Q07412P60174P60175P04789P52270P50921P00942
Entry nameTPIS_BACSTTPIS_CHICKTPIS_ECOLITPIS_PYRFUTPIS_PYRWOTPIS_LEIMETPIS_PLAFATPIS_HUMANTPIS_PANTRTPIS_TRYBBTPIS_TRYCRTPIS_VIBMATPIS_YEAST
ActivityD-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.D-glyceraldehyde 3-phosphate = glycerone phosphate.
SubunitHomodimer.Homodimer.Homodimer.Homotetramer (By similarity).Homotetramer.Homodimer.Homodimer.Homodimer.Homodimer (By similarity).Homodimer.Homodimer.Homodimer.Homodimer.
Subcellular locationCytoplasm (Probable).
Cytoplasm (Probable).Cytoplasm (Probable).Cytoplasm (Probable).Cytoplasm. Glycosome.


Glycosome.Glycosome.Cytoplasm (Probable).
Cofactor














SubstratesProductsintermediates
KEGG-idC00118C00111
CompoundD-Glyceraldehyde 3-phosphateGlycerone phosphate
Typecarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ion
1ag1OUnboundUnboundUnbound
1ag1TUnboundUnboundUnbound
1amkAUnboundUnboundTransition-state-analogue:PGA
1aw1AUnboundUnboundTransition-state-analogue:PGA
1aw1BUnboundUnboundTransition-state-analogue:PGA
1aw1DUnboundUnboundTransition-state-analogue:PGA
1aw1EUnboundUnboundTransition-state-analogue:PGA
1aw1GUnboundUnboundTransition-state-analogue:PGA
1aw1HUnboundUnboundTransition-state-analogue:PGA
1aw1JUnboundUnboundTransition-state-analogue:PGA
1aw1KUnboundUnboundTransition-state-analogue:PGA
1aw2AUnboundUnboundUnbound
1aw2BUnboundUnboundUnbound
1aw2DUnboundUnboundUnbound
1aw2EUnboundUnboundUnbound
1aw2GUnboundUnboundUnbound
1aw2HUnboundUnboundUnbound
1aw2JUnboundUnboundUnbound
1aw2KUnboundUnboundUnbound
1btmAUnboundUnboundTransition-state-analogue:PGA
1btmBUnboundUnboundTransition-state-analogue:PGA
1ci1AUnboundUnboundUnbound
1ci1BUnboundUnboundUnbound
1dkwAUnboundUnboundUnbound
1dkwBUnboundUnboundUnbound
1hg3AUnboundUnboundIntermediate-analogue:3PP
1hg3BUnboundUnboundIntermediate-analogue:3PP
1hg3CUnboundUnboundIntermediate-analogue:3PP
1hg3DUnboundUnboundIntermediate-analogue:3PP
1hg3EUnboundUnboundIntermediate-analogue:3PP
1hg3FUnboundUnboundIntermediate-analogue:3PP
1hg3GUnboundUnboundIntermediate-analogue:3PP
1hg3HUnboundUnboundIntermediate-analogue:3PP
1htiAUnboundUnboundTransition-state-analogue:PGA
1htiBUnboundUnboundTransition-state-analogue:PGA
1i45AUnboundUnboundUnbound
1i45BUnboundUnboundUnbound
1if2AAnalogue:129UnboundUnbound
1iigAUnboundUnboundUnbound
1iigBUnboundUnboundIntermediate-analogue:3PP
1iihAUnboundUnboundUnbound
1iihBAnalogue:3PGUnboundUnbound
1kv5AUnboundUnboundTransition-state-analogue:PGA
1kv5BUnboundUnboundTransition-state-analogue:PGA
1lyxAUnboundUnboundTransition-state-analogue:PGA
1lzoAUnboundUnboundUnbound
1lzoBUnboundUnboundTransition-state-analogue:PGA
1lzoCUnboundUnboundUnbound
1lzoDUnboundUnboundTransition-state-analogue:PGA
1m7oAAnalogue:3PGUnboundUnbound
1m7oBAnalogue:3PGUnboundUnbound
1m7pAAnalogue:G3HUnboundUnbound
1m7pBAnalogue:G3HUnboundUnbound
1ml1AUnboundUnboundTransition-state-analogue:PGA
1ml1CUnboundUnboundTransition-state-analogue:PGA
1ml1EUnboundUnboundTransition-state-analogue:PGA
1ml1GUnboundUnboundTransition-state-analogue:PGA
1ml1IUnboundUnboundTransition-state-analogue:PGA
1ml1KUnboundUnboundTransition-state-analogue:PGA
1mssAUnboundUnboundUnbound
1mssBUnboundUnboundUnbound
1n55AUnboundUnboundTransition-state-analogue:PGA
1neyAUnboundBound:13PUnbound
1neyBUnboundBound:13PUnbound
1nf0AUnboundBound:13PUnbound
1nf0BUnboundBound:13PUnbound
1o5xAUnboundUnboundIntermediate-analogue:3PY-PO3
1o5xBUnboundUnboundIntermediate-analogue:2PG
1qdsAUnboundUnboundTransition-state-analogue:PGA
1spqAUnboundUnboundUnbound
1spqBUnboundUnboundUnbound
1sq7AUnboundUnboundUnbound
1sq7BUnboundUnboundUnbound
1ssdAUnboundUnboundUnbound
1ssdBUnboundUnboundUnbound
1ssgAUnboundUnboundTransition-state-analogue:PGA
1ssgBUnboundUnboundTransition-state-analogue:PGA
1su5AUnboundUnboundTransition-state-analogue:PGA
1su5BUnboundUnboundTransition-state-analogue:PGA
1suxAUnboundUnboundUnbound
1suxBUnboundUnboundUnbound
1sw0AUnboundUnboundTransition-state-analogue:PGA
1sw0BUnboundUnboundTransition-state-analogue:PGA
1sw3AUnboundUnboundTransition-state-analogue:PGA
1sw3BUnboundUnboundTransition-state-analogue:PGA
1sw7AUnboundUnboundTransition-state-analogue:PGA
1sw7BUnboundUnboundTransition-state-analogue:PGA
1tcdAUnboundUnboundUnbound
1tcdBUnboundUnboundUnbound
1timAUnboundUnboundUnbound
1timBUnboundUnboundUnbound
1tmhAUnboundUnboundUnbound
1tmhBUnboundUnboundUnbound
1tmhCUnboundUnboundUnbound
1tmhDUnboundUnboundUnbound
1tpb1UnboundAnalogue:PGHUnbound
1tpb2UnboundAnalogue:PGHUnbound
1tpc1UnboundAnalogue:PGHUnbound
1tpc2UnboundAnalogue:PGHUnbound
1tpdAUnboundUnboundUnbound
1tpdBUnboundUnboundUnbound
1tpeAUnboundUnboundUnbound
1tpfAUnboundUnboundUnbound
1tpfBUnboundUnboundUnbound
1tph1UnboundAnalogue:PGHUnbound
1tph2UnboundAnalogue:PGHUnbound
1tpuAUnboundAnalogue:PGHUnbound
1tpuBUnboundAnalogue:PGHUnbound
1tpvAUnboundAnalogue:PGHUnbound
1tpvBUnboundAnalogue:PGHUnbound
1tpwAUnboundAnalogue:PGHUnbound
1tpwBUnboundAnalogue:PGHUnbound
1trdAUnboundAnalogue:PGHUnbound
1trdBUnboundAnalogue:PGHUnbound
1treAUnboundUnboundUnbound
1treBUnboundUnboundUnbound
1triAUnboundUnboundUnbound
1tsiAUnboundAnalogue:4PBUnbound
1tsiBUnboundUnboundUnbound
1ttiAUnboundUnboundTransition-state-analogue:PGA
1ttjAUnboundAnalogue:PGHUnbound
1vgaAUnboundUnboundUnbound
1vgaBUnboundUnboundUnbound
1vgaCUnboundUnboundUnbound
1vgaDUnboundUnboundUnbound
1woaAAnalogue:G2HUnboundUnbound
1woaBAnalogue:G2HUnboundUnbound
1woaCAnalogue:G2HUnboundUnbound
1woaDAnalogue:G2HUnboundUnbound
1wobAUnboundUnboundUnbound
1wobBUnboundUnboundUnbound
1wobCUnboundUnboundUnbound
1wobDUnboundUnboundUnbound
1ydvAUnboundUnboundUnbound
1ydvBUnboundUnboundUnbound
1ypiAUnboundUnboundUnbound
1ypiBUnboundUnboundUnbound
2btmAUnboundUnboundTransition-state-analogue:PGA
2btmBUnboundUnboundTransition-state-analogue:PGA
2ypiAUnboundUnboundTransition-state-analogue:PGA
2ypiBUnboundUnboundTransition-state-analogue:PGA
3timAUnboundUnboundUnbound
3timBUnboundUnboundUnbound
3ypiAUnboundAnalogue:PGHUnbound
3ypiBUnboundAnalogue:PGHUnbound
4timAUnboundUnboundUnbound
4timBUnboundUnboundIntermediate-analogue:2PG
5timAUnboundUnboundUnbound
5timBUnboundUnboundUnbound
6timAUnboundUnboundUnbound
6timBAnalogue:G3PUnboundUnbound
7timAUnboundAnalogue:PGHUnbound
7timBUnboundAnalogue:PGHUnbound
8timAUnboundUnboundUnbound
8timBUnboundUnboundUnbound

Active-site residues
resource
literature [42], [58], [76] & [102]
pdbCatalytic residuesModified residuescomment
1ag1OASN  11;LYS  13;HIS  95;GLU 167


1ag1TASN  11;LYS  13;HIS  95;GLU 167


1amkAASN  11;LYS  13;HIS  95;GLU 167


1aw1AASN   9;LYS  11;HIS  97;GLU 169


1aw1BASN   9;LYS  11;HIS  97;GLU 169


1aw1DASN   9;LYS  11;HIS  97;GLU 169


1aw1EASN   9;LYS  11;HIS  97;GLU 169


1aw1GASN   9;LYS  11;HIS  97;GLU 169


1aw1HASN   9;LYS  11;HIS  97;GLU 169


1aw1JASN   9;LYS  11;HIS  97;GLU 169


1aw1KASN   9;LYS  11;HIS  97;GLU 169


1aw2AASN   9;LYS  11;HIS  97;GLU 169


1aw2BASN   9;LYS  11;HIS  97;GLU 169


1aw2DASN   9;LYS  11;HIS  97;GLU 169


1aw2EASN   9;LYS  11;HIS  97;GLU 169


1aw2GASN   9;LYS  11;HIS  97;GLU 169


1aw2HASN   9;LYS  11;HIS  97;GLU 169


1aw2JASN   9;LYS  11;HIS  97;GLU 169


1aw2KASN   9;LYS  11;HIS  97;GLU 169


1btmAASN   8;LYS  10;HIS  94;GLU 166


1btmBASN   8;LYS  10;HIS  94;GLU 166


1ci1AASN  12;LYS  14;HIS  96;GLU 168


1ci1BASN  12;LYS  14;HIS  96;GLU 168


1dkwAASN  11;LYS  13;HIS  95;GLU 167


1dkwBASN  11;LYS  13;HIS  95;GLU 167


1hg3AASN  12;LYS  14;HIS  96;GLU 144


1hg3BASN  12;LYS  14;HIS  96;GLU 144


1hg3CASN  12;LYS  14;HIS  96;GLU 144


1hg3DASN  12;LYS  14;HIS  96;GLU 144


1hg3EASN  12;LYS  14;HIS  96;GLU 144


1hg3FASN  12;LYS  14;HIS  96;GLU 144


1hg3GASN  12;LYS  14;HIS  96;GLU 144


1hg3HASN  12;LYS  14;HIS  96;GLU 144


1htiAASN  11;LYS  13;HIS  95;GLU 165


1htiBASN  11;LYS  13;HIS  95;GLU 165


1i45AASN  10;LYS  12;HIS  95;GLU 165
FTR 168
mutant W90Y, W157F, W168FTR
1i45BASN  10;LYS  12;HIS  95;GLU 165
FTR 168
mutant W90Y, W157F, W168FTR
1if2AASN  11;LYS  13;HIS  95;GLU 167

mutant E65Q
1iigAASN  11;LYS  13;HIS  95;GLU 167


1iigBASN 311;LYS 313;HIS 395;GLU 467


1iihAASN  11;LYS  13;HIS  95;GLU 167


1iihBASN 311;LYS 313;HIS 395;GLU 467


1kv5AASN  11;LYS  13;HIS  95;GLU 167

mutant R191S
1kv5BASN  11;LYS  13;HIS  95;GLU 167

mutant R191S
1lyxAASN  10;LYS  12;HIS  95;GLU 165


1lzoAASN  10;LYS  12;HIS  95;GLU 165


1lzoBASN  10;LYS  12;HIS  95;GLU 165


1lzoCASN  10;LYS  12;HIS  95;GLU 165


1lzoDASN  10;LYS  12;HIS  95;GLU 165


1m7oAASN  10;LYS  12;HIS  95;GLU 165


1m7oBASN  10;LYS  12;HIS  95;GLU 165


1m7pAASN  10;LYS  12;HIS  95;GLU 165


1m7pBASN  10;LYS  12;HIS  95;GLU 165


1ml1AASN  11;LYS  13;HIS  95;GLU 167


1ml1CASN  11;LYS  13;HIS  95;GLU 167


1ml1EASN  11;LYS  13;HIS  95;GLU 167


1ml1GASN  11;LYS  13;HIS  95;GLU 167


1ml1IASN  11;LYS  13;HIS  95;GLU 167


1ml1KASN  11;LYS  13;HIS  95;GLU 167


1mssAASN  11;LYS  13;HIS  95;GLU 167

mutant F45S, V46S, 68-72 GNADALAS
1mssBASN  11;LYS  13;HIS  95;GLU 167

mutant F45S, V46S, 68-72 GNADALAS
1n55AASN  11;LYS  13;HIS  95;GLU 167

mutant E65Q
1neyAASN  10;LYS  12;HIS  95;GLU 165
FTR 168
mutant W90Y, W157F, W168FTR
1neyBASN  10;LYS  12;HIS  95;GLU 165
FTR 168
mutant W90Y, W157F, W168FTR
1nf0AASN  10;LYS  12;HIS  95;GLU 165
FTR 168
mutant W90Y, W157F, W168FTR
1nf0BASN  10;LYS  12;HIS  95;GLU 165
FTR 168
mutant W90Y, W157F, W168FTR
1o5xAASN  10;LYS  12;HIS  95;GLU 165

mutant A163V
1o5xBASN  10;LYS  12;HIS  95;GLU 165

mutant A163V
1qdsAASN  11;LYS  13;HIS  95;GLU 167

mutant E65Q
1spqAASN  11;LYS  13;HIS  95;GLU 165

mutant A176K
1spqBASN  11;LYS  13;HIS  95;GLU 165

mutant A176K
1sq7AASN  11;LYS  13;HIS  95;GLU 165

mutant K174L, T175W
1sq7BASN  11;LYS  13;HIS  95;GLU 165

mutant K174L, T175W
1ssdAASN  11;LYS  13;HIS  95;GLU 165

mutant K174Y, T175S, A176L
1ssdBASN  11;LYS  13;HIS  95;GLU 165

mutant K174Y, T175S, A176L
1ssgAASN  11;LYS  13;HIS  95;GLU 165

mutant K174Y, T175S, A176L
1ssgBASN  11;LYS  13;HIS  95;GLU 165

mutant K174Y, T175S, A176L
1su5AASN  11;LYS  13;HIS  95;GLU 165

mutant K174N, T175P, A176N
1su5BASN  11;LYS  13;HIS  95;GLU 165

mutant K174N, T175P, A176N
1suxAASN  12;LYS  14;HIS  96;GLU 168


1suxBASN  12;LYS  14;HIS  96;GLU 168


1sw0AASN  11;LYS  13;HIS  95;GLU 165

mutant K174L, T175W
1sw0BASN  11;LYS  13;HIS  95;GLU 165

mutant K174L, T175W
1sw3AASN  11;LYS  13;HIS  95;GLU 165

mutant T175V
1sw3BASN  11;LYS  13;HIS  95;GLU 165

mutant T175V
1sw7AASN  11;LYS  13;HIS  95;GLU 165

mutant K174N, T175S, A176S
1sw7BASN  11;LYS  13;HIS  95;GLU 165

mutant K174N, T175S, A176S
1tcdAASN  12;LYS  14;HIS  96;GLU 168


1tcdBASN  12;LYS  14;HIS  96;GLU 168


1timAASN  11;LYS  13;HIS  95;GLU 165


1timBASN  11;LYS  13;HIS  95;GLU 165


1tmhAASN  11;LYS  13;HIS  97;GLU 169

mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242
1tmhBASN  11;LYS  13;HIS  97;GLU 169

mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242
1tmhCASN  11;LYS  13;HIS  97;GLU 169

mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242
1tmhDASN  11;LYS  13;HIS  97;GLU 169

mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242
1tpb1ASN  11;LYS  13;HIS  95;       

mutant E165D
1tpb2ASN  11;LYS  13;HIS  95;       

mutant E165D
1tpc1ASN  11;LYS  13;HIS  95;       

mutant S96P, E165D
1tpc2ASN  11;LYS  13;HIS  95;       

mutant S96P, E165D
1tpdAASN  11;LYS  13;HIS  95;GLU 167


1tpdBASN  11;LYS  13;HIS  95;GLU 167


1tpeAASN  11;LYS  13;HIS  95;GLU 167


1tpfAASN  11;LYS  13;HIS  95;GLU 167


1tpfBASN  11;LYS  13;HIS  95;GLU 167


1tph1ASN  11;LYS  13;HIS  95;GLU 165


1tph2ASN  11;LYS  13;HIS  95;GLU 165


1tpuAASN  11;LYS  13;       ;GLU 165

mutant H95N
1tpuBASN  11;LYS  13;       ;GLU 165

mutant H95N
1tpvAASN  11;LYS  13;       ;GLU 165

mutant H95N, S96P
1tpvBASN  11;LYS  13;       ;GLU 165

mutant H95N, S96P
1tpwAASN  11;LYS  13;HIS  95;GLU 165

mutant S96P
1tpwBASN  11;LYS  13;HIS  95;GLU 165

mutant S96P
1trdAASN  11;LYS  13;HIS  95;GLU 167


1trdBASN  11;LYS  13;HIS  95;GLU 167


1treAASN  11;LYS  13;HIS  97;GLU 169


1treBASN  11;LYS  13;HIS  97;GLU 169


1triAASN  11;       ;HIS  95;GLU 167

mutant 68-82 GNADALAS, invisible K13
1tsiAASN  11;LYS  13;HIS  95;GLU 167


1tsiBASN  11;LYS  13;HIS  95;GLU 167


1ttiAASN  11;LYS  13;HIS  95;GLU 167

mutant I68G, A69N, K70A, S71D, P81A, A100W, deletion 73-79
1ttjAASN  11;       ;HIS  95;GLU 167

mutant F45S, V46S, invisible K13
1vgaAASN  10;LYS  12;HIS  95;GLU 165

mutant W168F
1vgaBASN  10;LYS  12;HIS  95;GLU 165

mutant W168F
1vgaCASN  10;LYS  12;HIS  95;GLU 165

mutant W168F
1vgaDASN  10;LYS  12;HIS  95;GLU 165

mutant W168F
1woaAASN  10;LYS  12;HIS  95;GLU 165

mutant A163V, W168F
1woaBASN  10;LYS  12;HIS  95;GLU 165

mutant A163V, W168F
1woaCASN  10;LYS  12;HIS  95;GLU 165

mutant A163V, W168F
1woaDASN  10;LYS  12;HIS  95;GLU 165

mutant A163V, W168F
1wobAASN  10;LYS  12;HIS  95;GLU 165

mutant A163V, W168F
1wobBASN  10;LYS  12;HIS  95;GLU 165

mutant A163V, W168F
1wobCASN  10;LYS  12;HIS  95;GLU 165

mutant A163V, W168F
1wobDASN  10;LYS  12;HIS  95;GLU 165

mutant A163V, W168F
1ydvAASN  10;LYS  12;HIS  95;GLU 165


1ydvBASN  10;LYS  12;HIS  95;GLU 165


1ypiAASN  10;LYS  12;HIS  95;GLU 165


1ypiBASN  10;LYS  12;HIS  95;GLU 165


2btmAASN   8;LYS  10;HIS  94;GLU 166


2btmBASN   8;LYS  10;HIS  94;GLU 166


2ypiAASN  10;LYS  12;HIS  95;GLU 165


2ypiBASN  10;LYS  12;HIS  95;GLU 165


3timAASN  11;LYS  13;HIS  95;GLU 167


3timBASN  11;LYS  13;HIS  95;GLU 167


3ypiAASN  10;LYS  12;       ;GLU 165

mutant H95Q
3ypiBASN  10;LYS  12;       ;GLU 165

mutant H95Q
4timAASN  11;LYS  13;HIS  95;GLU 167


4timBASN  11;LYS  13;HIS  95;GLU 167


5timAASN  11;LYS  13;HIS  95;GLU 167


5timBASN  11;LYS  13;HIS  95;GLU 167


6timAASN  11;LYS  13;HIS  95;GLU 167


6timBASN  11;LYS  13;HIS  95;GLU 167


7timAASN  10;LYS  12;HIS  95;GLU 165


7timBASN  10;LYS  12;HIS  95;GLU 165


8timAASN  11;LYS  13;HIS  95;GLU 165


8timBASN  11;LYS  13;HIS  95;GLU 165



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.1, p.159-161, p.168-170
[4]Fig.1, p.604, p.607-612
[5]p.120
[7]Fig.1
[9]Fig.1, Fig.4
[10]Scheme I, p.3187
[11]Fig.1, p.678
[12]Scheme I
[13]Fig.1, Fig.2, Fig.4
[14]Scheme I, Scheme II, p.3016-3017
[15]Fig.1, Fig.2
[21]FIG.1
[27]Scheme I
[28]Fig.3, p.241-243
[29]Fig.1
[33]Fig.1
[34]Fig.1
[35]Fig.1
[40]Fig.3, p.314
[42]Fig.2
[43]Fig.1
[44]

[45]Fig.1
[50]Fig.1
[53]Fig.1
[54]Fig.1
[56]Fig.1, p.232-234
[58]Scheme 1, Scheme 3, Fig.8
[67]Fig.1, p.4395-4396
[69]SCHEME 1
[76]Fig.1, p.5194
[78]Fig.1
[87]Scheme 1, Fig.1
[88]Scheme 1
[90]SCHEME I, SCHEME II, Fig.6
[93]FIG.1
[94]FIG.1, p.52468-52469
[95]Scheme 1, p.47
[97]Fig.1, Fig.3, p.52-54
[99]

[102]Fig.1, p.229-230

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND REVISION.
Medline ID75175220
PubMed ID1134550
JournalNature
Year1975
Volume255
Pages609-14
AuthorsBanner DW, Bloomer AC, Petsko GA, Phillips DC, Pogson CI, Wilson IA, Corran PH, Furth AJ, Milman JD, Offord RE, Priddle JD, Waley SG
TitleStructure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data.
Related Swiss-protP00940
[2]
CommentsX-RAY CRYSTALLOGRAPHY.
Medline ID77044751
PubMed ID985462
JournalBiochem Biophys Res Commun
Year1976
Volume72
Pages146-55
AuthorsBanner DW, Bloomer A, Petsko GA, Phillips DC, Wilson IA
TitleAtomic coordinates for triose phosphate isomerase from chicken muscle.
Related PDB1tim
Related Swiss-protP00940
[3]
CommentsX-ray crystallography
PubMed ID6115415
JournalPhilos Trans R Soc Lond B Biol Sci
Year1981
Volume293
Pages159-71
AuthorsAlber T, Banner DW, Bloomer AC, Petsko GA, Phillips D, Rivers PS, Wilson IA
TitleOn the three-dimensional structure and catalytic mechanism of triose phosphate isomerase.
Related PDB1ml1
[4]
CommentsREVIEW.
Medline ID88295752
PubMed ID3331346
JournalCold Spring Harb Symp Quant Biol
Year1987
Volume52
Pages603-13
AuthorsAlber TC, Davenport RC Jr, Giammona DA, Lolis E, Petsko GA, Ringe D
TitleCrystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
Related Swiss-protP00942
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID88118904
PubMed ID3430602
JournalJ Mol Biol
Year1987
Volume198
Pages109-21
AuthorsWierenga RK, Kalk KH, Hol WG
TitleStructure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 A resolution.
Related Swiss-protP04789
[6]
PubMed ID2260979
JournalBiochem Biophys Res Commun
Year1990
Volume173
Pages736-40
AuthorsSchnackerz KD, Kuan TK, Goux WJ, Gracy RW
TitlePhosphorus-31 nuclear magnetic resonance spectroscopy reveals two conformational forms of chloroacetol phosphate-bound triosephosphate isomerase.
[7]
PubMed ID2361134
JournalBiochemistry
Year1990
Volume29
Pages4099-108
AuthorsBlacklow SC, Knowles JR
TitleHow can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID90373768
PubMed ID2204417
JournalBiochemistry
Year1990
Volume29
Pages6609-18
AuthorsLolis E, Alber T, Davenport RC, Rose D, Hartman FC, Petsko GA
TitleStructure of yeast triosephosphate isomerase at 1.9-A resolution.
Related PDB1ypi
Related Swiss-protP00942
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE.
Medline ID90373769
PubMed ID2204418
JournalBiochemistry
Year1990
Volume29
Pages6619-25
AuthorsLolis E, Petsko GA
TitleCrystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
Related PDB2ypi
Related Swiss-protP00942
[10]
PubMed ID2185832
JournalBiochemistry
Year1990
Volume29
Pages3186-94
AuthorsPompliano DL, Peyman A, Knowles JR
TitleStabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase.
[11]
PubMed ID2217142
JournalProtein Eng
Year1990
Volume3
Pages677-90
AuthorsDaggett V, Kollman PA
TitleMolecular dynamics simulations of active site mutants of triosephosphate isomerase.
[12]
PubMed ID1883832
JournalBiochemistry
Year1991
Volume30
Pages8470-6
AuthorsBlacklow SC, Liu KD, Knowles JR
TitleStepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase.
[13]
CommentsX-ray crystallography
PubMed ID2043623
JournalBiochemistry
Year1991
Volume30
Pages5821-6
AuthorsDavenport RC, Bash PA, Seaton BA, Karplus M, Petsko GA, Ringe D
TitleStructure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway.
Related PDB7tim
[14]
CommentsX-ray crystallography
PubMed ID2007138
JournalBiochemistry
Year1991
Volume30
Pages3011-9
AuthorsKomives EA, Chang LC, Lolis E, Tilton RF, Petsko GA, Knowles JR
TitleElectrophilic catalysis in triosephosphate isomerase: the role of histidine-95.
Related PDB3ypi
[15]
PubMed ID2069953
JournalBiochemistry
Year1991
Volume30
Pages6948-56
AuthorsLodi PJ, Knowles JR
TitleNeutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications.
[16]
PubMed ID1814699
JournalCiba Found Symp
Year1991
Volume161
Pages91-103; discussion 103-7
AuthorsKollman PA, Daggett V, Dang LX
TitleThe application of computational methods to the study of enzyme catalysis by triose-phosphate isomerase and stabilities of variants of bacteriophage T4 lysozyme.
[17]
PubMed ID2065677
JournalEur J Biochem
Year1991
Volume199
Pages231-8
AuthorsSchnackerz KD, Gracy RW
TitleProbing the catalytic sites of triosephosphate isomerase by 31P-NMR with reversibly and irreversibly binding substrate analogues.
[18]
CommentsX-ray crystallography
PubMed ID2040290
JournalEur J Biochem
Year1991
Volume198
Pages53-7
AuthorsVerlinde CL, Noble ME, Kalk KH, Groendijk H, Wierenga RK, Hol WG
TitleAnion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate.
Related PDB1ag1
[19]
CommentsX-ray crystallography
PubMed ID1895291
JournalJ Med Chem
Year1991
Volume34
Pages2709-18
AuthorsNoble ME, Verlinde CL, Groendijk H, Kalk KH, Wierenga RK, Hol WG
TitleCrystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: a critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate.
Related PDB4tim
[20]
CommentsX-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
Medline ID91350193
PubMed ID1880808
JournalJ Mol Biol
Year1991
Volume220
Pages995-1015
AuthorsWierenga RK, Noble ME, Vriend G, Nauche S, Hol WG
TitleRefined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex.
Related PDB5tim
Related Swiss-protP04789
[21]
PubMed ID2005961
JournalNature
Year1991
Volume350
Pages121-4
AuthorsKnowles JR
TitleEnzyme catalysis: not different, just better.
[22]
CommentsX-ray crystallography
PubMed ID2062828
JournalProteins
Year1991
Volume10
Pages50-69
AuthorsNoble ME, Wierenga RK, Lambeir AM, Opperdoes FR, Thunnissen AM, Kalk KH, Groendijk H, Hol WG
TitleThe adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
Related PDB6tim,1iig,1iih
[23]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE.
PubMed ID2062827
JournalProteins
Year1991
Volume10
Pages33-49
AuthorsWierenga RK, Noble ME, Postma JP, Groendijk H, Kalk KH, Hol WG, Opperdoes FR
TitleThe crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase.
Related PDB3tim
[24]
PubMed ID1536574
JournalArch Biochem Biophys
Year1992
Volume293
Pages382-90
AuthorsSun AQ, Yuksel KU, Gracy RW
TitleRelationship between the catalytic center and the primary degradation site of triosephosphate isomerase: effects of active site modification and deamidation.
[25]
PubMed ID1586170
JournalArch Biochem Biophys
Year1992
Volume295
Pages421-8
AuthorsSun AQ, Yuksel KU, Rao GS, Gracy RW
TitleEffects of active site modification and reversible dissociation on the secondary structure of triosephosphate isomerase.
[26]
PubMed ID1390633
JournalBiochemistry
Year1992
Volume31
Pages8488-94
AuthorsSampson NS, Knowles JR
TitleSegmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase.
[27]
PubMed ID1390632
JournalBiochemistry
Year1992
Volume31
Pages8482-7
AuthorsSampson NS, Knowles JR
TitleSegmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase.
[28]
PubMed ID1290934
JournalFaraday Discuss
Year1992
Volume(93)
Pages239-48
AuthorsKarplus M, Evanseck JD, Joseph D, Bash PA, Field MJ
TitleSimulation analysis of triose phosphate isomerase: conformational transition and catalysis.
[29]
PubMed ID1628747
JournalFEBS Lett
Year1992
Volume306
Pages80-4
AuthorsHennig M, Schlesier B, Dauter Z, Pfeffer S, Betzel C, Hohne WE, Wilson KS
TitleA TIM barrel protein without enzymatic activity? Crystal-structure of narbonin at 1.8 A resolution.
[30]
PubMed ID1639191
JournalFEBS Lett
Year1992
Volume307
Pages34-9
AuthorsWierenga RK, Borchert TV, Noble ME
TitleCrystallographic binding studies with triosephosphate isomerases: conformational changes induced by substrate and substrate-analogues.
[31]
PubMed ID1400336
JournalJ Biol Chem
Year1992
Volume267
Pages20168-74
AuthorsSun AQ, Yuksel KU, Gracy RW
TitleInteractions between the catalytic centers and subunit interface of triosephosphate isomerase probed by refolding, active site modification, and subunit exchange.
[32]
CommentsX-RAY CRYSTALLOGRAPHY.
Medline ID92235847
PubMed ID1569570
JournalJ Mol Biol
Year1992
Volume224
Pages1115-26
AuthorsWierenga RK, Noble ME, Davenport RC
TitleComparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase.
Related Swiss-protP00940,P00942,P04789
[33]
CommentsX-ray crystallography
PubMed ID1304889
JournalProtein Sci
Year1992
Volume1
Pages1578-84
AuthorsVerlinde CL, Witmans CJ, Pijning T, Kalk KH, Hol WG, Callens M, Opperdoes FR
TitleStructure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation.
Related PDB1tsi
[34]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed ID15299515
JournalActa Crystallogr D Biol Crystallogr
Year1993
Volume49(Pt 4)
Pages403-17
AuthorsNoble ME.M, Zeelen JP, Wierenga RK, Mainfroid V, Goraj K, Gohimont A-C, Martial JA
TitleStructure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution.
Related PDB1tre
Related Swiss-protP0A858
[35]
PubMed ID8476863
JournalBiochemistry
Year1993
Volume32
Pages4338-43
AuthorsLodi PJ, Knowles JR
TitleDirect evidence for the exploitation of an alpha-helix in the catalytic mechanism of triosephosphate isomerase.
[36]
PubMed ID8431552
JournalBiophys J
Year1993
Volume64
Pages9-15
AuthorsWade RC, Davis ME, Luty BA, Madura JD, McCammon JA
TitleGating of the active site of triose phosphate isomerase: Brownian dynamics simulations of flexible peptide loops in the enzyme.
[37]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND REVISION TO 203.
Medline ID93170303
PubMed ID8436128
JournalEur J Biochem
Year1993
Volume211
Pages703-10
AuthorsBorchert TV, Pratt K, Zeelen JP, Callens M, Noble ME, Opperdoes FR, Michels PA, Wierenga RK
TitleOverexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant.
Related Swiss-protP04789
[38]
PubMed ID8262920
JournalJ Biol Chem
Year1993
Volume268
Pages26872-8
AuthorsSun AQ, Yuksel KU, Gracy RW
TitleLimited proteolysis of triose-phosphate isomerase and characterization of the catalytically active peptide complex.
[39]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID94143343
PubMed ID8309937
JournalProtein Eng
Year1993
Volume6
Pages893-900
AuthorsMainfroid V, Goraj K, Rentier-Delrue F, Houbrechts A, Loiseau A, Gohimont AC, Noble ME, Borchert TV, Wierenga RK, Martial JA
TitleReplacing the (beta alpha)-unit 8 of E.coli TIM with its chicken homologue leads to a stable and active hybrid enzyme.
Related Swiss-protP0A858
[40]
CommentsX-ray crystallography
PubMed ID8356028
JournalProteins
Year1993
Volume16
Pages311-26
AuthorsNoble ME, Zeelen JP, Wierenga RK
TitleStructures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism.
Related PDB1tpd,1trd
[41]
PubMed ID8204630
JournalBiochemistry
Year1994
Volume33
Pages6960-5
AuthorsGarza-Ramos G, Tuena de Gomez-Puyou M, Gomez-Puyou A, Yuksel KU, Gracy RW
TitleDeamidation of triosephosphate isomerase in reverse micelles: effects of water on catalysis and molecular wear and tear.
[42]
PubMed ID8130194
JournalBiochemistry
Year1994
Volume33
Pages2815-23
AuthorsJoseph-McCarthy D, Lolis E, Komives EA, Petsko GA
TitleCrystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site.
[43]
PubMed ID7907502
JournalBiochemistry
Year1994
Volume33
Pages2824-9
AuthorsJoseph-McCarthy D, Rost LE, Komives EA, Petsko GA
TitleCrystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid.
[44]
PubMed ID8130193
JournalBiochemistry
Year1994
Volume33
Pages2809-14
AuthorsLodi PJ, Chang LC, Knowles JR, Komives EA
TitleTriosephosphate isomerase requires a positively charged active site: the role of lysine-12.
[45]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID94176473
PubMed ID8130195
JournalBiochemistry
Year1994
Volume33
Pages2830-7
AuthorsZhang Z, Sugio S, Komives EA, Liu KD, Knowles JR, Petsko GA, Ringe D
TitleCrystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution.
Related PDB1tph
Related Swiss-protP00940
[46]
PubMed ID7906272
JournalJ Biol Chem
Year1994
Volume269
Pages5005-8
AuthorsYuksel KU, Sun AQ, Gracy RW, Schnackerz KD
TitleThe hinged lid of yeast triose-phosphate isomerase. Determination of the energy barrier between the two conformations.
[47]
CommentsX-ray crystallography
PubMed ID7809033
JournalProtein Eng
Year1994
Volume7
Pages945-51
AuthorsKishan R, Zeelen JP, Noble ME, Borchert TV, Mainfroid V, Goraj K, Martial JA, Wierenga RK
TitleModular mutagenesis of a TIM-barrel enzyme: the crystal structure of a chimeric E. coli TIM having the eighth beta alpha-unit replaced by the equivalent unit of chicken TIM.
Related PDB1tmh
[48]
CommentsX-ray crystallography
PubMed ID8061607
JournalProtein Sci
Year1994
Volume3
Pages779-87
AuthorsKishan KV, Zeelen JP, Noble ME, Borchert TV, Wierenga RK
TitleComparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
Related PDB1tpe,1tpf
[49]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID94339841
PubMed ID8061610
JournalProtein Sci
Year1994
Volume3
Pages810-21
AuthorsMande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WG
TitleCrystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme.
Related PDB1hti
Related Swiss-protP60174
[50]
CommentsX-ray crystallography
PubMed ID7577950
JournalBiochemistry
Year1995
Volume34
Pages13612-21
AuthorsKomives EA, Lougheed JC, Liu K, Sugio S, Zhang Z, Petsko GA, Ringe D
TitleThe structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules.
Related PDB1tpb,1tpc
[51]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID96164392
PubMed ID8580851
JournalProtein Sci
Year1995
Volume4
Pages2594-604
AuthorsDelboni LF, Mande SC, Rentier-Delrue F, Mainfroid V, Turley S, Vellieux FM, Martial JA, Hol WG
TitleCrystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions.
Related PDB1btm
Related Swiss-protP00943
[52]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS.
Medline ID96000857
PubMed ID8591044
JournalStructure
Year1995
Volume3
Pages669-79
AuthorsBorchert TV, Kishan KV, Zeelen JP, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga RK
TitleThree new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8.
Related PDB1tri,1tti,1ttj
Related Swiss-protP04789
[53]
CommentsX-ray crystallography
PubMed ID8952501
JournalBiochemistry
Year1996
Volume35
Pages15474-84
AuthorsKomives EA, Lougheed JC, Zhang Z, Sugio S, Narayana N, Xuong NH, Petsko GA, Ringe D
TitleThe structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase.
Related PDB1tpu,1tpv
[54]
PubMed ID8626554
JournalJ Biol Chem
Year1996
Volume271
Pages10010-6
AuthorsAqvist J, Fothergill M
TitleComputer simulation of the triosephosphate isomerase catalyzed reaction.
[55]
PubMed ID8745400
JournalProtein Sci
Year1996
Volume5
Pages229-39
AuthorsSchliebs W, Thanki N, Eritja R, Wierenga R
TitleActive site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies.
[56]
PubMed ID8811738
JournalProteins
Year1996
Volume25
Pages225-36
AuthorsPerakyla M, Pakkanen TA
TitleAb initio models for receptor-ligand interactions in proteins. 4. Model assembly study of the catalytic mechanism of triosephosphate isomerase.
[57]
PubMed ID9126273
JournalArch Biochem Biophys
Year1997
Volume340
Pages27-35
AuthorsTalent JM, Zvaigzne AI, Agrawal N, Gracy RW
TitleEffect of active-site modification on the terminal marking deamidation of triosephosphate isomerase.
[58]
PubMed ID9398185
JournalBiochemistry
Year1997
Volume36
Pages14661-75
AuthorsHarris TK, Abeygunawardana C, Mildvan AS
TitleNMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase.
[59]
PubMed ID9245397
JournalBiochemistry
Year1997
Volume36
Pages9655-62
AuthorsSchliebs W, Thanki N, Jaenicke R, Wierenga RK
TitleA double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.
[60]
PubMed ID9089815
JournalProtein Eng
Year1997
Volume10
Pages159-67
AuthorsThanki N, Zeelen JP, Mathieu M, Jaenicke R, Abagyan RA, Wierenga RK, Schliebs W
TitleProtein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop.
[61]
PubMed ID9144796
JournalProteins
Year1997
Volume28
Pages109-16
AuthorsKobayashi N, Yamato T, Go N
TitleMechanical property of a TIM-barrel protein.
[62]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PGK, AND REVISIONS.
Medline ID98046096
PubMed ID9384563
JournalStructure
Year1997
Volume5
Pages1475-83
AuthorsAuerbach G, Huber R, Grattinger M, Zaiss K, Schurig H, Jaenicke R, Jacob U
TitleClosed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability.
Related Swiss-protP36204
[63]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID97410385
PubMed ID9261072
JournalStructure
Year1997
Volume5
Pages751-61
AuthorsVelanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR
TitleTriosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design.
Related PDB1ydv
Related Swiss-protQ07412
[64]
CommentsNUCLEOTIDE SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed ID9442062
JournalJ Biol Chem
Year1998
Volume273
Pages2199-206
AuthorsAlvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D
TitleTriose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
Related PDB1aw1,1aw2
Related Swiss-protP50921
[65]
CommentsX-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
Medline ID98437380
PubMed ID9761683
JournalJ Mol Biol
Year1998
Volume283
Pages193-203
AuthorsMaldonado E, Soriano-Garcia M, Moreno A, Cabrera N, Garza-Ramos G, de Gomez-Puyou M, Gomez-Puyou A, Perez-Montfort R
TitleDifferences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes.
Related PDB1tcd
Related Swiss-protP52270
[66]
PubMed ID10194326
JournalBiochemistry
Year1999
Volume38
Pages4114-20
AuthorsPerez-Montfort R, Garza-Ramos G, Alcantara GH, Reyes-Vivas H, Gao XG, Maldonado E, de Gomez-Puyou MT, Gomez-Puyou A
TitleDerivatization of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi as probe of the interrelationship between the catalytic sites and the dimer interface.
[67]
PubMed ID10194358
JournalBiochemistry
Year1999
Volume38
Pages4389-97
AuthorsZhang Z, Komives EA, Sugio S, Blacklow SC, Narayana N, Xuong NH, Stock AM, Petsko GA, Ringe D
TitleThe role of water in the catalytic efficiency of triosephosphate isomerase.
[68]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID99315861
PubMed ID10383424
JournalJ Biol Chem
Year1999
Volume274
Pages19181-7
AuthorsAlvarez M, Wouters J, Maes D, Mainfroid V, Rentier-Delrue F, Wyns L, Depiereux E, Martial JA
TitleLys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures.
Related PDB2btm
Related Swiss-protP00943
[69]
PubMed ID10507008
JournalMethods Enzymol
Year1999
Volume308
Pages246-76
AuthorsShan SO, Herschlag D
TitleHydrogen bonding in enzymatic catalysis: analysis of energetic contributions.
[70]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID99398662
PubMed ID10468562
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages10062-7
AuthorsGao XG, Maldonado E, Perez-Montfort R, Garza-Ramos G, de Gomez-Puyou MT, Gomez-Puyou A, Rodriguez-Romero A
TitleCrystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane.
Related PDB1ci1
Related Swiss-protP52270
[71]
CommentsX-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
Medline ID99249704
PubMed ID10235625
JournalProtein Eng
Year1999
Volume12
Pages243-50
AuthorsWilliams JC, Zeelen JP, Neubauer G, Vriend G, Backmann J, Michels PA, Lambeir AM, Wierenga RK
TitleStructural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.
Related PDB1amk
Related Swiss-protP48499
[72]
CommentsX-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF TIM.
Medline ID20058648
PubMed ID10591103
JournalProteins
Year1999
Volume37
Pages441-53
AuthorsMaes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, Wierenga RK
TitleThe crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
Related PDB1b9b
Related Swiss-protP36204
[73]
PubMed ID10591103
JournalProteins
Year1999
Volume37
Pages441-53
AuthorsMaes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, Wierenga RK
TitleThe crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
[74]
PubMed ID10957646
JournalActa Crystallogr D Biol Crystallogr
Year2000
Volume56
Pages1201-3
AuthorsWouters J, Maes D
TitleIdentification of a potential metal cation-pi binding site in the structure of a thermophilic Bacillus stearothermophilus triosephosphate isomerase mutant.
[75]
CommentsX-ray crystallography
PubMed ID10785370
JournalEur J Biochem
Year2000
Volume267
Pages2516-24
AuthorsLambeir AM, Backmann J, Ruiz-Sanz J, Filimonov V, Nielsen JE, Kursula I, Norledge BV, Wierenga RK
TitleThe ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase.
Related PDB1qds
[76]
CommentsX-ray crystallography
PubMed ID11589711
JournalEur J Biochem
Year2001
Volume268
Pages5189-96
AuthorsKursula I, Partanen S, Lambeir AM, Antonov DM, Augustyns K, Wierenga RK
TitleStructural determinants for ligand binding and catalysis of triosephosphate isomerase.
Related PDB1if2
[77]
CommentsX-ray crystallography
PubMed ID11419952
JournalJ Mol Biol
Year2001
Volume310
Pages271-80
AuthorsRozovsky S, Jogl G, Tong L, McDermott AE
TitleSolution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.
Related PDB1i45
[78]
PubMed ID11419951
JournalJ Mol Biol
Year2001
Volume310
Pages259-70
AuthorsRozovsky S, McDermott AE
TitleThe time scale of the catalytic loop motion in triosephosphate isomerase.
[79]
CommentsX-ray crystallography
PubMed ID11243785
JournalJ Mol Biol
Year2001
Volume306
Pages745-57
AuthorsWalden H, Bell GS, Russell RJ, Siebers B, Hensel R, Taylor GL
TitleTiny TIM: a small, tetrameric, hyperthermostable triosephosphate isomerase.
Related PDB1hg3
Related Swiss-protP62003
[80]
PubMed ID11286559
JournalJ Mol Biol
Year2001
Volume307
Pages1103-12
AuthorsXiang J, Sun J, Sampson NS
TitleThe importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase.
[81]
PubMed ID11342710
JournalProtein Eng
Year2001
Volume14
Pages149-55
AuthorsSaab-Rincon G, Juarez VR, Osuna J, Sanchez F, Soberon X
TitleDifferent strategies to recover the activity of monomeric triosephosphate isomerase by directed evolution.
[82]
CommentsX-ray crystallography
PubMed ID11151009
JournalProteins
Year2001
Volume42
Pages383-9
AuthorsNorledge BV, Lambeir AM, Abagyan RA, Rottmann A, Fernandez AM, Filimonov VV, Peter MG, Wierenga RK
TitleModeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificity.
Related PDB1dkw
[83]
CommentsX-ray crystallography
PubMed ID12454456
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages1992-2000
AuthorsParthasarathy S, Balaram H, Balaram P, Murthy MR
TitleStructures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state.
Related PDB1m7o,1m7p
[84]
PubMed ID11914068
JournalBiochemistry
Year2002
Volume41
Pages4230-8
AuthorsHernandez-Alcantara G, Garza-Ramos G, Hernandez GM, Gomez-Puyou A, Perez-Montfort R
TitleCatalysis and stability of triosephosphate isomerase from Trypanosoma brucei with different residues at position 14 of the dimer interface. Characterization of a catalytically competent monomeric enzyme.
[85]
CommentsX-ray crystallography
PubMed ID12403619
JournalBiochemistry
Year2002
Volume41
Pages13178-88
AuthorsParthasarathy S, Ravindra G, Balaram H, Balaram P, Murthy MR
TitleStructure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state.
Related PDB1lyx,1lzo
[86]
CommentsX-ray crystallography
PubMed ID11997014
JournalFEBS Lett
Year2002
Volume518
Pages39-42
AuthorsKursula I, Partanen S, Lambeir AM, Wierenga RK
TitleThe importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis.
Related PDB1kv5
[87]
PubMed ID11902900
JournalJ Am Chem Soc
Year2002
Volume124
Pages3093-124
AuthorsCui Q, Karplus M
TitleQuantum mechanics/molecular mechanics studies of triosephosphate isomerase-catalyzed reactions: effect of geometry and tunneling on proton-transfer rate constants.
[88]
PubMed ID12475328
JournalJ Am Chem Soc
Year2002
Volume124
Pages14871-8
AuthorsZhang X, Harrison DH, Cui Q
TitleFunctional specificities of methylglyoxal synthase and triosephosphate isomerase: a combined QM/MM analysis.
[89]
PubMed ID12185208
JournalJ Biol Chem
Year2002
Volume277
Pages30968-75
AuthorsSilverman JA, Harbury PB
TitleRapid mapping of protein structure, interactions, and ligand binding by misincorporation proton-alkyl exchange.
[90]
PubMed ID14631822
JournalAdv Protein Chem
Year2003
Volume66
Pages315-72
AuthorsCui Q, Karplus M
TitleCatalysis and specificity in enzymes: a study of triosephosphate isomerase and comparison with methyl glyoxal synthase.
[91]
PubMed ID12472469
JournalBiochem J
Year2003
Volume370
Pages785-92
AuthorsNajera H, Costas M, Fernandez-Velasco DA
TitleThermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme.
[92]
PubMed ID12627960
JournalBiochemistry
Year2003
Volume42
Pages2941-51
AuthorsDesamero R, Rozovsky S, Zhadin N, McDermott A, Callender R
TitleActive site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation.
[93]
CommentsX-ray crystallography
PubMed ID12522213
JournalJ Biol Chem
Year2003
Volume278
Pages9544-51
AuthorsKursula I, Wierenga RK
TitleCrystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution.
Related PDB1n55
[94]
CommentsX-ray crystallography
PubMed ID14563846
JournalJ Biol Chem
Year2003
Volume278
Pages52461-70
AuthorsParthasarathy S, Eaazhisai K, Balaram H, Balaram P, Murthy MR
TitleStructure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution.
Related PDB1o5x
[95]
PubMed ID12483674
JournalJ Comput Chem
Year2003
Volume24
Pages46-56
AuthorsAlagona G, Ghio C, Kollman PA
TitleThe intramolecular mechanism for the second proton transfer in triosephosphate isomerase (TIM): a QM/FE approach.
[96]
PubMed ID14643664
JournalJ Mol Biol
Year2003
Volume334
Pages1023-41
AuthorsAparicio R, Ferreira ST, Polikarpov I
TitleClosed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity.
[97]
CommentsX-ray crystallography
PubMed ID12509510
JournalProc Natl Acad Sci U S A
Year2003
Volume100
Pages50-5
AuthorsJogl G, Rozovsky S, McDermott AE, Tong L
TitleOptimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
Related PDB1ney,1nf0
[98]
PubMed ID15023076
JournalBiochemistry
Year2004
Volume43
Pages3255-63
AuthorsGonzalez-Mondragon E, Zubillaga RA, Saavedra E, Chanez-Cardenas ME, Perez-Montfort R, Hernandez-Arana A
TitleConserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability.
[99]
PubMed ID15350130
JournalBiochemistry
Year2004
Volume43
Pages11436-45
AuthorsXiang J, Jung JY, Sampson NS
TitleEntropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase.
[100]
PubMed ID15324804
JournalChem Biol
Year2004
Volume11
Pages1037-42
AuthorsTousignant A, Pelletier JN
TitleProtein motions promote catalysis.
[101]
CommentsX-ray crystallography
PubMed ID15465054
JournalJ Mol Biol
Year2004
Volume343
Pages671-84
AuthorsEaazhisai K, Balaram H, Balaram P, Murthy MR
TitleStructures of unliganded and inhibitor complexes of W168F, a Loop6 hinge mutant of Plasmodium falciparum triosephosphate isomerase: observation of an intermediate position of loop6.
Related PDB1vga,1woa,1wob
[102]
PubMed ID15001364
JournalJ Mol Biol
Year2004
Volume337
Pages227-39
AuthorsGuallar V, Jacobson M, McDermott A, Friesner RA
TitleComputational modeling of the catalytic reaction in triosephosphate isomerase.
[103]
CommentsX-ray crystallography
PubMed ID15321726
JournalJ Mol Biol
Year2004
Volume341
Pages1355-1365
AuthorsTellez-Valencia A, Olivares-Illana V, Hernandez-Santoyo A, Perez-Montfort R, Costas M, Rodriguez-Romero A, Lopez-Calahorra F, Tuena de Gomez-Puyou M, Gomez-Puyou A
TitleInactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface
Related PDB1sux
[104]
CommentsX-ray crystallography
PubMed ID15166315
JournalProtein Eng Des Sel
Year2004
Volume17
Pages375-82
AuthorsKursula I, Salin M, Sun J, Norledge BV, Haapalainen AM, Sampson NS, Wierenga RK
TitleUnderstanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase.
Related PDB1spq,1sq7,1ssd,1ssg,1su5,1sw0,1sw3,1sw7
[105]
PubMed ID15103619
JournalProteins
Year2004
Volume55
Pages548-57
AuthorsShukla A, Guptasarma P
TitleFolding of beta/alpha-unit scrambled forms of S. cerevisiae triosephosphate isomerase: Evidence for autonomy of substructure formation and plasticity of hydrophobic and hydrogen bonding interactions in core of (beta/alpha)8-barrel.
[106]
PubMed ID15707966
JournalBiochem Biophys Res Commun
Year2005
Volume328
Pages922-8
AuthorsEspinoza-Fonseca LM, Trujillo-Ferrara JG
TitleStructural considerations for the rational design of selective anti-trypanosomal agents: the role of the aromatic clusters at the interface of triosephosphate isomerase dimer.

comments
According to the literature [4], [13], [14], [15], [58], [90], [94], [95] & [102], there have been three possible mechanisms proposed to date, as follows:
(1) Glu165 (of 1ypi) acts as a general acid-base to transfer a (pro-R) proton from C1 to C2 (of substrate), whereas His95 acts as a general acid-base or proton shuttle to transfer a proton from O1 to O2.
(2) Intramolecular proton transfer from O1 to O2.
(3) Glu165 acts as a general acid-base to transfer a (pro-R) proton from C1 to O2 (of substrate), and then transfers a proton from O1 to C2.
According to the literature, as His95 is neutral, which rarely acts as a general base. Moreover, His95 may disturb the intramolecular proton transfer (see [102]. Thus, the mechanism (3) is most likely.
According to the literature [42], [58], [76] & [102], this enzyme catalyzes two successive isomerizations (or shifts of double-bond).
(A) Isomerization; Shift of double-bond from carbonyl group to adjacent C=C.
(A1) Glu165 acts as as a general base to deprotonate the C1 atom of substrate (G3P), which leads to the formation of an enodilate intermediate with double-bond between the C1 and C2 atoms. Here, His95 and Lys12 stabilize the negative charge on the enediolate (or the O2 atom).
(A2) Glu165 acts as a general acid to protonate the O1 atom, leading to the enediol intermediate.
(B) Isomerization; Shift of double-bond from C=C to carbonyl group.
(B1) Glu165 acts as a general base to deprotonate the O1 hydroxyl atom, leading to the enediolate intermediate. His95 and Asn10 stabilize the negative charge on the O1 atom.
(B2) Glu165 acts as a general acid to protonate the C2 atom, giving the product (GP).

createdupdated
2005-05-112009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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