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

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PubMed ID2185832
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[14]
CommentsX-ray crystallography
PubMed ID2007138
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Volume30
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PubMed ID2069953
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PubMed ID2040290
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Related PDB1ag1
[19]
CommentsX-ray crystallography
PubMed ID1895291
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Volume34
Pages2709-18
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Related PDB4tim
[20]
CommentsX-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
Medline ID91350193
PubMed ID1880808
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Year1991
Volume220
Pages995-1015
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Related PDB5tim
Related Swiss-protP04789
[21]
PubMed ID2005961
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Year1991
Volume350
Pages121-4
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TitleEnzyme catalysis: not different, just better.
[22]
CommentsX-ray crystallography
PubMed ID2062828
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Volume10
Pages50-69
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Related PDB6tim,1iig,1iih
[23]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE.
PubMed ID2062827
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Year1991
Volume10
Pages33-49
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Related PDB3tim
[24]
PubMed ID1536574
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Year1992
Volume293
Pages382-90
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TitleRelationship between the catalytic center and the primary degradation site of triosephosphate isomerase: effects of active site modification and deamidation.
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PubMed ID1586170
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Year1992
Volume295
Pages421-8
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TitleEffects of active site modification and reversible dissociation on the secondary structure of triosephosphate isomerase.
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PubMed ID1390633
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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
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Year1992
Volume31
Pages8482-7
AuthorsSampson NS, Knowles JR
TitleSegmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase.
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PubMed ID1290934
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Pages239-48
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PubMed ID1639191
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PubMed ID1400336
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CommentsX-RAY CRYSTALLOGRAPHY.
Medline ID92235847
PubMed ID1569570
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Related Swiss-protP00940,P00942,P04789
[33]
CommentsX-ray crystallography
PubMed ID1304889
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Volume1
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PubMed ID15299515
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Related PDB1tre
Related Swiss-protP0A858
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PubMed ID8476863
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Year1993
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CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND REVISION TO 203.
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PubMed ID8436128
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PubMed ID8262920
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Volume268
Pages26872-8
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Related Swiss-protP0A858
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CommentsX-ray crystallography
PubMed ID8356028
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Related PDB1tpd,1trd
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PubMed ID8204630
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PubMed ID7907502
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Volume33
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PubMed ID8130193
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Year1994
Volume33
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Medline ID94176473
PubMed ID8130195
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Related PDB1tph
Related Swiss-protP00940
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PubMed ID7906272
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Volume269
Pages5005-8
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[47]
CommentsX-ray crystallography
PubMed ID7809033
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Volume7
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Related PDB1tmh
[48]
CommentsX-ray crystallography
PubMed ID8061607
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Year1994
Volume3
Pages779-87
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Related PDB1tpe,1tpf
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CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID94339841
PubMed ID8061610
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Related PDB1hti
Related Swiss-protP60174
[50]
CommentsX-ray crystallography
PubMed ID7577950
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Volume34
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Related PDB1tpb,1tpc
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Medline ID96164392
PubMed ID8580851
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Related PDB1btm
Related Swiss-protP00943
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CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS.
Medline ID96000857
PubMed ID8591044
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Year1995
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Related PDB1tri,1tti,1ttj
Related Swiss-protP04789
[53]
CommentsX-ray crystallography
PubMed ID8952501
JournalBiochemistry
Year1996
Volume35
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PubMed ID8626554
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AuthorsAqvist J, Fothergill M
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Volume10
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PubMed ID9144796
JournalProteins
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CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PGK, AND REVISIONS.
Medline ID98046096
PubMed ID9384563
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Pages1475-83
AuthorsAuerbach G, Huber R, Grattinger M, Zaiss K, Schurig H, Jaenicke R, Jacob U
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Related Swiss-protP36204
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CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID97410385
PubMed ID9261072
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Year1997
Volume5
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Related PDB1ydv
Related Swiss-protQ07412
[64]
CommentsNUCLEOTIDE SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed ID9442062
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AuthorsAlvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D
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Related PDB1aw1,1aw2
Related Swiss-protP50921
[65]
CommentsX-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
Medline ID98437380
PubMed ID9761683
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Year1998
Volume283
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Related PDB1tcd
Related Swiss-protP52270
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PubMed ID10194326
JournalBiochemistry
Year1999
Volume38
Pages4114-20
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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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