EzCatDB: T00043

DB codeT00043
RLCP classification3.130.90020.2100
8.113.915310.365
CATH domainDomain 13.40.1380.20
Domain 23.20.20.60Catalytic domain
Domain 32.40.33.10Catalytic domain
E.C.2.7.1.40
CSA1pkn
MACiEM0326

CATH domainRelated DB codes (homologues)
3.20.20.60S00241,T00217,S00197,S00242,D00477

Enzyme Name
Swiss-protKEGG

P0AD61P00549Q27686P11974P11979P30613P14618
Protein namePyruvate kinase IPyruvate kinase 1Pyruvate kinasePyruvate kinase isozymes M1/M2Pyruvate kinase isozyme M1Pyruvate kinase isozymes R/LPyruvate kinase isozymes M1/M2pyruvate kinase
phosphoenolpyruvate kinase
phosphoenol transphosphorylase
SynonymsEC 2.7.1.40
PK-1
PK 1
EC 2.7.1.40
PK
EC 2.7.1.40
EC 2.7.1.40
Pyruvate kinase muscle isozyme
EC 2.7.1.40
Pyruvate kinase muscle isozyme
EC 2.7.1.40
R-type/L-type pyruvate kinase
Red cell/liver pyruvate kinase
Pyruvate kinase 1
EC 2.7.1.40
Pyruvate kinase muscle isozyme
Pyruvate kinase 2/3
Cytosolic thyroid hormone-binding protein
CTHBP
THBP1

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00230Purine metabolism
MAP00620Pyruvate metabolism
MAP00710Carbon fixation in photosynthetic organisms

Swiss-prot:Accession NumberP0AD61P00549Q27686P11974P11979P30613P14618
Entry nameKPYK1_ECOLIKPYK1_YEASTKPYK_LEIMEKPYM_RABITKPYM_FELCAKPYR_HUMANKPYM_HUMAN
ActivityATP + pyruvate = ADP + phosphoenolpyruvate.ATP + pyruvate = ADP + phosphoenolpyruvate.ATP + pyruvate = ADP + phosphoenolpyruvate.ATP + pyruvate = ADP + phosphoenolpyruvate.ATP + pyruvate = ADP + phosphoenolpyruvate.ATP + pyruvate = ADP + phosphoenolpyruvate.ATP + pyruvate = ADP + phosphoenolpyruvate.
SubunitHomotetramer.Homotetramer.Homotetramer.Interacts with HERC1 (By similarity). Homotetramer.Interacts with HERC1 (By similarity). Homotetramer.Homotetramer.Homotetramer. Interacts with HERC1.
Subcellular location






CofactorMagnesium.,Potassium.Magnesium.,Potassium.Magnesium.,Potassium.Magnesium.,Potassium.Magnesium.,Potassium.Magnesium.,Potassium.Magnesium.,Potassium.


CofactorsSubstratesProducts
KEGG-idC00305C00238C00008C00074C00002C00022
CompoundMagnesiumPotassiumADPPhosphoenolpyruvateATPPyruvate
Typedivalent metal (Ca2+, Mg2+)univalent metal (Na+, K+)amine group,nucleotidecarboxyl group,phosphate group/phosphate ionamine group,nucleotidecarbohydrate,carboxyl group
1e0tA01UnboundUnboundUnboundUnboundUnboundUnbound
1e0tB01UnboundUnboundUnboundUnboundUnboundUnbound
1e0tC01UnboundUnboundUnboundUnboundUnboundUnbound
1e0tD01UnboundUnboundUnboundUnboundUnboundUnbound
1e0uA01UnboundUnboundUnboundUnboundUnboundUnbound
1e0uB01UnboundUnboundUnboundUnboundUnboundUnbound
1e0uC01UnboundUnboundUnboundUnboundUnboundUnbound
1e0uD01UnboundUnboundUnboundUnboundUnboundUnbound
1pkyA01UnboundUnboundUnboundUnboundUnboundUnbound
1pkyB01UnboundUnboundUnboundUnboundUnboundUnbound
1pkyC01UnboundUnboundUnboundUnboundUnboundUnbound
1pkyD01UnboundUnboundUnboundUnboundUnboundUnbound
1a3wA01UnboundUnboundUnboundUnboundUnboundUnbound
1a3wB01UnboundUnboundUnboundUnboundUnboundUnbound
1a3xA01UnboundUnboundUnboundUnboundUnboundUnbound
1a3xB01UnboundUnboundUnboundUnboundUnboundUnbound
1pklA01UnboundUnboundUnboundUnboundUnboundUnbound
1pklB01UnboundUnboundUnboundUnboundUnboundUnbound
1pklC01UnboundUnboundUnboundUnboundUnboundUnbound
1pklD01UnboundUnboundUnboundUnboundUnboundUnbound
1pklE01UnboundUnboundUnboundUnboundUnboundUnbound
1pklF01UnboundUnboundUnboundUnboundUnboundUnbound
1pklG01UnboundUnboundUnboundUnboundUnboundUnbound
1pklH01UnboundUnboundUnboundUnboundUnboundUnbound
1a49A01UnboundUnboundUnboundUnboundUnboundUnbound
1a49B01UnboundUnboundUnboundUnboundUnboundUnbound
1a49C01UnboundUnboundUnboundUnboundUnboundUnbound
1a49D01UnboundUnboundUnboundUnboundUnboundUnbound
1a49E01UnboundUnboundUnboundUnboundUnboundUnbound
1a49F01UnboundUnboundUnboundUnboundUnboundUnbound
1a49G01UnboundUnboundUnboundUnboundUnboundUnbound
1a49H01UnboundUnboundUnboundUnboundUnboundUnbound
1a5uA01UnboundUnboundUnboundUnboundUnboundUnbound
1a5uB01UnboundUnboundUnboundUnboundUnboundUnbound
1a5uC01UnboundUnboundUnboundUnboundUnboundUnbound
1a5uD01UnboundUnboundUnboundUnboundUnboundUnbound
1a5uE01UnboundUnboundUnboundUnboundUnboundUnbound
1a5uF01UnboundUnboundUnboundUnboundUnboundUnbound
1a5uG01UnboundUnboundUnboundUnboundUnboundUnbound
1a5uH01UnboundUnboundUnboundUnboundUnboundUnbound
1aqfA01UnboundUnboundUnboundUnboundUnboundUnbound
1aqfB01UnboundUnboundUnboundUnboundUnboundUnbound
1aqfC01UnboundUnboundUnboundUnboundUnboundUnbound
1aqfD01UnboundUnboundUnboundUnboundUnboundUnbound
1aqfE01UnboundUnboundUnboundUnboundUnboundUnbound
1aqfF01UnboundUnboundUnboundUnboundUnboundUnbound
1aqfG01UnboundUnboundUnboundUnboundUnboundUnbound
1aqfH01UnboundUnboundUnboundUnboundUnboundUnbound
1f3wA01UnboundUnboundUnboundUnboundUnboundUnbound
1f3wB01UnboundUnboundUnboundUnboundUnboundUnbound
1f3wC01UnboundUnboundUnboundUnboundUnboundUnbound
1f3wD01UnboundUnboundUnboundUnboundUnboundUnbound
1f3wE01UnboundUnboundUnboundUnboundUnboundUnbound
1f3wF01UnboundUnboundUnboundUnboundUnboundUnbound
1f3wG01UnboundUnboundUnboundUnboundUnboundUnbound
1f3wH01UnboundUnboundUnboundUnboundUnboundUnbound
1f3xA01UnboundUnboundUnboundUnboundUnboundUnbound
1f3xB01UnboundUnboundUnboundUnboundUnboundUnbound
1f3xC01UnboundUnboundUnboundUnboundUnboundUnbound
1f3xD01UnboundUnboundUnboundUnboundUnboundUnbound
1f3xE01UnboundUnboundUnboundUnboundUnboundUnbound
1f3xF01UnboundUnboundUnboundUnboundUnboundUnbound
1f3xG01UnboundUnboundUnboundUnboundUnboundUnbound
1f3xH01UnboundUnboundUnboundUnboundUnboundUnbound
1pknA01UnboundUnboundUnboundUnboundUnboundUnbound
1pkmA01UnboundUnboundUnboundUnboundUnboundUnbound
1liuA01UnboundUnboundUnboundUnboundUnboundUnbound
1liuB01UnboundUnboundUnboundUnboundUnboundUnbound
1liuC01UnboundUnboundUnboundUnboundUnboundUnbound
1liuD01UnboundUnboundUnboundUnboundUnboundUnbound
1liwA01UnboundUnboundUnboundUnboundUnboundUnbound
1liwB01UnboundUnboundUnboundUnboundUnboundUnbound
1liwC01UnboundUnboundUnboundUnboundUnboundUnbound
1liwD01UnboundUnboundUnboundUnboundUnboundUnbound
1lixA01UnboundUnboundUnboundUnboundUnboundUnbound
1lixB01UnboundUnboundUnboundUnboundUnboundUnbound
1lixC01UnboundUnboundUnboundUnboundUnboundUnbound
1lixD01UnboundUnboundUnboundUnboundUnboundUnbound
1liyA01UnboundUnboundUnboundUnboundUnboundUnbound
1liyB01UnboundUnboundUnboundUnboundUnboundUnbound
1liyC01UnboundUnboundUnboundUnboundUnboundUnbound
1liyD01UnboundUnboundUnboundUnboundUnboundUnbound
1t5aA01UnboundUnboundUnboundUnboundUnboundUnbound
1t5aB01UnboundUnboundUnboundUnboundUnboundUnbound
1t5aC01UnboundUnboundUnboundUnboundUnboundUnbound
1t5aD01UnboundUnboundUnboundUnboundUnboundUnbound
1zjhA01UnboundUnboundUnboundUnboundUnboundUnbound
1e0tA02UnboundUnboundUnboundUnboundUnboundUnbound
1e0tB02UnboundUnboundUnboundUnboundUnboundUnbound
1e0tC02UnboundUnboundUnboundUnboundUnboundUnbound
1e0tD02UnboundUnboundUnboundUnboundUnboundUnbound
1e0uA02UnboundUnboundUnboundUnboundUnboundUnbound
1e0uB02UnboundUnboundUnboundUnboundUnboundUnbound
1e0uC02UnboundUnboundUnboundUnboundUnboundUnbound
1e0uD02UnboundUnboundUnboundUnboundUnboundUnbound
1pkyA02UnboundUnboundUnboundUnboundUnboundUnbound
1pkyB02UnboundUnboundUnboundUnboundUnboundUnbound
1pkyC02UnboundUnboundUnboundUnboundUnboundUnbound
1pkyD02UnboundUnboundUnboundUnboundUnboundUnbound
1a3wA02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1a3wB02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1a3xA02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1a3xB02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1pklA02UnboundUnboundUnboundUnboundUnboundUnbound
1pklB02UnboundUnboundUnboundUnboundUnboundUnbound
1pklC02UnboundUnboundUnboundUnboundUnboundUnbound
1pklD02UnboundUnboundUnboundUnboundUnboundUnbound
1pklE02UnboundUnboundUnboundUnboundUnboundUnbound
1pklF02UnboundUnboundUnboundUnboundUnboundUnbound
1pklG02UnboundUnboundUnboundUnboundUnboundUnbound
1pklH02UnboundUnboundUnboundUnboundUnboundUnbound
1a49A02Bound:2x_MGBound:__KUnboundUnboundBound:ATPAnalogue:OXL
1a49B02Bound:_MGBound:__KUnboundUnboundUnboundAnalogue:OXL
1a49C02Bound:2x_MGBound:__KUnboundUnboundBound:ATPAnalogue:OXL
1a49D02Bound:2x_MGBound:__KUnboundUnboundBound:ATPAnalogue:OXL
1a49E02Bound:2x_MGBound:__KUnboundUnboundBound:ATPAnalogue:OXL
1a49F02Bound:2x_MGBound:__KUnboundUnboundBound:ATPAnalogue:OXL
1a49G02Bound:2x_MGBound:__KUnboundUnboundBound:ATPAnalogue:OXL
1a49H02Bound:_MGBound:__KUnboundUnboundUnboundAnalogue:OXL
1a5uA02Bound:2x_MGAnalogue:_NAUnboundUnboundBound:ATPAnalogue:OXL
1a5uB02Bound:_MGAnalogue:_NAUnboundUnboundUnboundAnalogue:OXL
1a5uC02Bound:2x_MGAnalogue:_NAUnboundUnboundBound:ATPAnalogue:OXL
1a5uD02Bound:2x_MGAnalogue:_NAUnboundUnboundBound:ATPAnalogue:OXL
1a5uE02Bound:2x_MGAnalogue:_NAUnboundUnboundBound:ATPAnalogue:OXL
1a5uF02Bound:2x_MGAnalogue:_NAUnboundUnboundBound:ATPAnalogue:OXL
1a5uG02Bound:2x_MGAnalogue:_NAUnboundUnboundBound:ATPAnalogue:OXL
1a5uH02Bound:_MGAnalogue:_NAUnboundUnboundUnboundAnalogue:OXL
1aqfA02Bound:_MGBound:__KUnboundBound:PEQUnboundUnbound
1aqfB02Bound:_MGBound:__KUnboundBound:PEQUnboundUnbound
1aqfC02Bound:_MGBound:__KUnboundBound:PEQUnboundUnbound
1aqfD02Bound:_MGBound:__KUnboundBound:PEQUnboundUnbound
1aqfE02Bound:_MGBound:__KUnboundBound:PEQUnboundUnbound
1aqfF02Bound:_MGBound:__KUnboundBound:PEQUnboundUnbound
1aqfG02Bound:_MGBound:__KUnboundBound:PEQUnboundUnbound
1aqfH02Bound:_MGBound:__KUnboundBound:PEQUnboundUnbound
1f3wA02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3wB02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3wC02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3wD02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3wE02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3wF02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3wG02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3wH02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3xA02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3xB02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3xC02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3xD02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3xE02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3xF02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3xG02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1f3xH02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1pknA02Analogue:_MNBound:__KUnboundUnboundUnboundBound:PYR
1pkmA02UnboundUnboundUnboundUnboundUnboundUnbound
1liuA02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liuB02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liuC02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liuD02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liwA02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liwB02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liwC02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liwD02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1lixA02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1lixB02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1lixC02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1lixD02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liyA02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liyB02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liyC02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1liyD02Analogue:_MNBound:__KUnboundAnalogue:PGAUnboundUnbound
1t5aA02Bound:_MGBound:__KUnboundUnboundUnboundAnalogue:OXL
1t5aB02Bound:_MGBound:__KUnboundUnboundUnboundAnalogue:OXL
1t5aC02Bound:_MGBound:__KUnboundUnboundUnboundAnalogue:OXL
1t5aD02Bound:_MGBound:__KUnboundUnboundUnboundAnalogue:OXL
1zjhA02UnboundUnboundUnboundUnboundUnboundUnbound
1e0tA03UnboundUnboundUnboundUnboundUnboundUnbound
1e0tB03UnboundUnboundUnboundUnboundUnboundUnbound
1e0tC03UnboundUnboundUnboundUnboundUnboundUnbound
1e0tD03UnboundUnboundUnboundUnboundUnboundUnbound
1e0uA03UnboundUnboundUnboundUnboundUnboundUnbound
1e0uB03UnboundUnboundUnboundUnboundUnboundUnbound
1e0uC03UnboundUnboundUnboundUnboundUnboundUnbound
1e0uD03UnboundUnboundUnboundUnboundUnboundUnbound
1pkyA03UnboundUnboundUnboundUnboundUnboundUnbound
1pkyB03UnboundUnboundUnboundUnboundUnboundUnbound
1pkyC03UnboundUnboundUnboundUnboundUnboundUnbound
1pkyD03UnboundUnboundUnboundUnboundUnboundUnbound
1a3wA03UnboundUnboundUnboundUnboundUnboundUnbound
1a3wB03UnboundUnboundUnboundUnboundUnboundUnbound
1a3xA03UnboundUnboundUnboundUnboundUnboundUnbound
1a3xB03UnboundUnboundUnboundUnboundUnboundUnbound
1pklA03UnboundUnboundUnboundUnboundUnboundUnbound
1pklB03UnboundUnboundUnboundUnboundUnboundUnbound
1pklC03UnboundUnboundUnboundUnboundUnboundUnbound
1pklD03UnboundUnboundUnboundUnboundUnboundUnbound
1pklE03UnboundUnboundUnboundUnboundUnboundUnbound
1pklF03UnboundUnboundUnboundUnboundUnboundUnbound
1pklG03UnboundUnboundUnboundUnboundUnboundUnbound
1pklH03UnboundUnboundUnboundUnboundUnboundUnbound
1a49A03UnboundUnboundUnboundUnboundUnboundUnbound
1a49B03UnboundUnboundUnboundUnboundUnboundUnbound
1a49C03UnboundUnboundUnboundUnboundUnboundUnbound
1a49D03UnboundUnboundUnboundUnboundUnboundUnbound
1a49E03UnboundUnboundUnboundUnboundUnboundUnbound
1a49F03UnboundUnboundUnboundUnboundUnboundUnbound
1a49G03UnboundUnboundUnboundUnboundUnboundUnbound
1a49H03UnboundUnboundUnboundUnboundUnboundUnbound
1a5uA03UnboundUnboundUnboundUnboundUnboundUnbound
1a5uB03UnboundUnboundUnboundUnboundUnboundUnbound
1a5uC03UnboundUnboundUnboundUnboundUnboundUnbound
1a5uD03UnboundUnboundUnboundUnboundUnboundUnbound
1a5uE03UnboundUnboundUnboundUnboundUnboundUnbound
1a5uF03UnboundUnboundUnboundUnboundUnboundUnbound
1a5uG03UnboundUnboundUnboundUnboundUnboundUnbound
1a5uH03UnboundUnboundUnboundUnboundUnboundUnbound
1aqfA03UnboundUnboundUnboundUnboundUnboundUnbound
1aqfB03UnboundUnboundUnboundUnboundUnboundUnbound
1aqfC03UnboundUnboundUnboundUnboundUnboundUnbound
1aqfD03UnboundUnboundUnboundUnboundUnboundUnbound
1aqfF03UnboundUnboundUnboundUnboundUnboundUnbound
1aqfG03UnboundUnboundUnboundUnboundUnboundUnbound
1aqfH03UnboundUnboundUnboundUnboundUnboundUnbound
1f3wA03UnboundUnboundUnboundUnboundUnboundUnbound
1f3wB03UnboundUnboundUnboundUnboundUnboundUnbound
1f3wC03UnboundUnboundUnboundUnboundUnboundUnbound
1f3wD03UnboundUnboundUnboundUnboundUnboundUnbound
1f3wE03UnboundUnboundUnboundUnboundUnboundUnbound
1f3wF03UnboundUnboundUnboundUnboundUnboundUnbound
1f3wG03UnboundUnboundUnboundUnboundUnboundUnbound
1f3wH03UnboundUnboundUnboundUnboundUnboundUnbound
1f3xA03UnboundUnboundUnboundUnboundUnboundUnbound
1f3xB03UnboundUnboundUnboundUnboundUnboundUnbound
1f3xC03UnboundUnboundUnboundUnboundUnboundUnbound
1f3xD03UnboundUnboundUnboundUnboundUnboundUnbound
1f3xE03UnboundUnboundUnboundUnboundUnboundUnbound
1f3xF03UnboundUnboundUnboundUnboundUnboundUnbound
1f3xG03UnboundUnboundUnboundUnboundUnboundUnbound
1f3xH03UnboundUnboundUnboundUnboundUnboundUnbound
1pknA03UnboundUnboundUnboundUnboundUnboundUnbound
1pkmA03UnboundUnboundUnboundUnboundUnboundUnbound
1liuA03UnboundUnboundUnboundUnboundUnboundUnbound
1liuB03UnboundUnboundUnboundUnboundUnboundUnbound
1liuC03UnboundUnboundUnboundUnboundUnboundUnbound
1liuD03UnboundUnboundUnboundUnboundUnboundUnbound
1liwA03UnboundUnboundUnboundUnboundUnboundUnbound
1liwB03UnboundUnboundUnboundUnboundUnboundUnbound
1liwC03UnboundUnboundUnboundUnboundUnboundUnbound
1liwD03UnboundUnboundUnboundUnboundUnboundUnbound
1lixA03UnboundUnboundUnboundUnboundUnboundUnbound
1lixB03UnboundUnboundUnboundUnboundUnboundUnbound
1lixC03UnboundUnboundUnboundUnboundUnboundUnbound
1lixD03UnboundUnboundUnboundUnboundUnboundUnbound
1liyA03UnboundUnboundUnboundUnboundUnboundUnbound
1liyB03UnboundUnboundUnboundUnboundUnboundUnbound
1liyC03UnboundUnboundUnboundUnboundUnboundUnbound
1liyD03UnboundUnboundUnboundUnboundUnboundUnbound
1t5aA03UnboundUnboundUnboundUnboundUnboundUnbound
1t5aB03UnboundUnboundUnboundUnboundUnboundUnbound
1t5aC03UnboundUnboundUnboundUnboundUnboundUnbound
1t5aD03UnboundUnboundUnboundUnboundUnboundUnbound
1zjhA03UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [10], [33], [36]
pdbCatalytic residuesCofactor-binding residuescomment
1e0tA01


1e0tB01


1e0tC01


1e0tD01


1e0uA01


1e0uB01


1e0uC01


1e0uD01


1pkyA01


1pkyB01


1pkyC01


1pkyD01


1a3wA01


1a3wB01


1a3xA01


1a3xB01


1pklA01


1pklB01


1pklC01


1pklD01


1pklE01


1pklF01


1pklG01


1pklH01


1a49A01


1a49B01


1a49C01


1a49D01


1a49E01


1a49F01


1a49G01


1a49H01


1a5uA01


1a5uB01


1a5uC01


1a5uD01


1a5uE01


1a5uF01


1a5uG01


1a5uH01


1aqfA01


1aqfB01


1aqfC01


1aqfD01


1aqfE01


1aqfF01


1aqfG01


1aqfH01


1f3wA01


1f3wB01


1f3wC01


1f3wD01


1f3wE01


1f3wF01


1f3wG01


1f3wH01


1f3xA01

mutant S402P
1f3xB01

mutant S402P
1f3xC01

mutant S402P
1f3xD01

mutant S402P
1f3xE01

mutant S402P
1f3xF01

mutant S402P
1f3xG01

mutant S402P
1f3xH01

mutant S402P
1pknA01


1pkmA01


1liuA01


1liuB01


1liuC01


1liuD01


1liwA01


1liwB01


1liwC01


1liwD01


1lixA01


1lixB01


1lixC01


1lixD01


1liyA01


1liyB01


1liyC01


1liyD01


1t5aA01


1t5aB01


1t5aC01


1t5aD01


1zjhA01


1e0tA02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)
mutant Q279M, R292D
1e0tB02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)
mutant Q279M, R292D
1e0tC02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)
mutant Q279M, R292D
1e0tD02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)
mutant Q279M, R292D
1e0uA02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)
mutant R271L, Q279M
1e0uB02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)
mutant R271L, Q279M
1e0uC02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)
mutant R271L, Q279M
1e0uD02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)
mutant R271L, Q279M
1pkyA02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)

1pkyB02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)

1pkyC02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)

1pkyD02ARG   32;LYS  220;THR  278;SER  312;GLU  314
ASN   34;SER   36;ASP   66;THR   67(Potassium);GLU  222;ASP  246(Magnesium)

1a3wA02ARG   49;LYS  240;THR  298;SER  332;GLU  334
ASN   51;SER   53;ASP   84;THR   85(Potassium);GLU  242;ASP  266(Magnesium)

1a3wB02ARG   49;LYS  240;THR  298;SER  332;GLU  334
ASN   51;SER   53;ASP   84;THR   85(Potassium);GLU  242;ASP  266(Magnesium)

1a3xA02ARG   49;LYS  240;THR  298;SER  332;GLU  334
ASN   51;SER   53;ASP   84;THR   85(Potassium);GLU  242;ASP  266(Magnesium)

1a3xB02ARG   49;LYS  240;THR  298;SER  332;GLU  334
ASN   51;SER   53;ASP   84;THR   85(Potassium);GLU  242;ASP  266(Magnesium)

1pklA02ARG   49;LYS  238;THR  296;SER  330;GLU  332
ASN   51;SER   53;ASP   83;THR   84(Potassium);GLU  240;ASP  264(Magnesium)

1pklB02ARG   49;LYS  238;THR  296;SER  330;GLU  332
ASN   51;SER   53;ASP   83;THR   84(Potassium);GLU  240;ASP  264(Magnesium)

1pklC02ARG   49;LYS  238;THR  296;SER  330;GLU  332
ASN   51;SER   53;ASP   83;THR   84(Potassium);GLU  240;ASP  264(Magnesium)

1pklD02ARG   49;LYS  238;THR  296;SER  330;GLU  332
ASN   51;SER   53;ASP   83;THR   84(Potassium);GLU  240;ASP  264(Magnesium)

1pklE02ARG   49;LYS  238;THR  296;SER  330;GLU  332
ASN   51;SER   53;ASP   83;THR   84(Potassium);GLU  240;ASP  264(Magnesium)

1pklF02ARG   49;LYS  238;THR  296;SER  330;GLU  332
ASN   51;SER   53;ASP   83;THR   84(Potassium);GLU  240;ASP  264(Magnesium)

1pklG02ARG   49;LYS  238;THR  296;SER  330;GLU  332
ASN   51;SER   53;ASP   83;THR   84(Potassium);GLU  240;ASP  264(Magnesium)

1pklH02ARG   49;LYS  238;THR  296;SER  330;GLU  332
ASN   51;SER   53;ASP   83;THR   84(Potassium);GLU  240;ASP  264(Magnesium)

1a49A02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1a49B02ARG  672;LYS  869;THR  927;SER  961;GLU  963
ASN  674;SER  676;ASP  712;THR  713(Potassium);GLU  871;ASP  895(Magnesium)

1a49C02ARG 1272;LYS 1469;THR 1527;SER 1561;GLU 1563
ASN 1274;SER 1276;ASP 1312;THR 1313(Potassium);GLU 1471;ASP 1495(Magnesium)

1a49D02ARG 1872;LYS 2069;THR 2127;SER 2161;GLU 2163
ASN 1874;SER 1876;ASP 1912;THR 1913(Potassium);GLU 2071;ASP 2095(Magnesium)

1a49E02ARG 3072;LYS 3269;THR 3327;SER 3361;GLU 3363
ASN 3074;SER 3076;ASP 3112;THR 3113(Potassium);GLU 3271;ASP 3295(Magnesium)

1a49F02ARG 3672;LYS 3869;THR 3927;SER 3961;GLU 3963
ASN 3674;SER 3676;ASP 3712;THR 3713(Potassium);GLU 3871;ASP 3895(Magnesium)

1a49G02ARG 4272;LYS 4469;THR 4527;SER 4561;GLU 4563
ASN 4274;SER 4276;ASP 4312;THR 4313(Potassium);GLU 4471;ASP 4495(Magnesium)

1a49H02ARG 4872;LYS 5069;THR 5127;SER 5161;GLU 5163
ASN 4874;SER 4876;ASP 4912;THR 4913(Potassium);GLU 5071;ASP 5095(Magnesium)

1a5uA02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1a5uB02ARG  672;LYS  869;THR  927;SER  961;GLU  963
ASN  674;SER  676;ASP  712;THR  713(Potassium);GLU  871;ASP  895(Magnesium)

1a5uC02ARG 1272;LYS 1469;THR 1527;SER 1561;GLU 1563
ASN 1274;SER 1276;ASP 1312;THR 1313(Potassium);GLU 1471;ASP 1495(Magnesium)

1a5uD02ARG 1872;LYS 2069;THR 2127;SER 2161;GLU 2163
ASN 1874;SER 1876;ASP 1912;THR 1913(Potassium);GLU 2071;ASP 2095(Magnesium)

1a5uE02ARG 3072;LYS 3269;THR 3327;SER 3361;GLU 3363
ASN 3074;SER 3076;ASP 3112;THR 3113(Potassium);GLU 3271;ASP 3295(Magnesium)

1a5uF02ARG 3672;LYS 3869;THR 3927;SER 3961;GLU 3963
ASN 3674;SER 3676;ASP 3712;THR 3713(Potassium);GLU 3871;ASP 3895(Magnesium)

1a5uG02ARG 4272;LYS 4469;THR 4527;SER 4561;GLU 4563
ASN 4274;SER 4276;ASP 4312;THR 4313(Potassium);GLU 4471;ASP 4495(Magnesium)

1a5uH02ARG 4872;LYS 5069;THR 5127;SER 5161;GLU 5163
ASN 4874;SER 4876;ASP 4912;THR 4913(Potassium);GLU 5071;ASP 5095(Magnesium)

1aqfA02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1aqfB02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1aqfC02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1aqfD02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1aqfE02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1aqfF02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1aqfG02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1aqfH02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1f3wA02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1f3wB02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1f3wC02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1f3wD02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1f3wE02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1f3wF02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1f3wG02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1f3wH02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1f3xA02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Manganese)

1f3xB02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Manganese)

1f3xC02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Manganese)

1f3xD02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Manganese)

1f3xE02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Manganese)

1f3xF02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Manganese)

1f3xG02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Manganese)

1f3xH02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Manganese)

1pknA02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Manganese)

1pkmA02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1liuA02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liuB02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liuC02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liuD02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liwA02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liwB02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liwC02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liwD02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1lixA02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1lixB02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1lixC02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1lixD02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liyA02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liyB02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liyC02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1liyD02ARG  116;LYS  313;THR  371;SER  405;GLU  407
ASN  118;SER  120;ASP  156;THR  157(Potassium);GLU  315;ASP  339(Magnesium)

1t5aA02ARG   73;LYS  270;THR  328;SER  362;GLU  364
ASN   75;SER   77;ASP  113;THR  114(Potassium);GLU  272;ASP  296(Magnesium)

1t5aB02ARG   73;LYS  270;THR  328;SER  362;GLU  364
ASN   75;SER   77;ASP  113;THR  114(Potassium);GLU  272;ASP  296(Magnesium)

1t5aC02ARG   73;LYS  270;THR  328;SER  362;GLU  364
ASN   75;SER   77;ASP  113;THR  114(Potassium);GLU  272;ASP  296(Magnesium)

1t5aD02ARG   73;LYS  270;THR  328;SER  362;GLU  364
ASN   75;SER   77;ASP  113;THR  114(Potassium);GLU  272;ASP  296(Magnesium)

1zjhA02ARG   72;LYS  269;THR  327;SER  361;GLU  363
ASN   74;SER   76;ASP  112;THR  113(Potassium);GLU  271;ASP  295(Magnesium)

1e0tA03ARG   73


1e0tB03ARG   73


1e0tC03ARG   73


1e0tD03ARG   73


1e0uA03ARG   73


1e0uB03ARG   73


1e0uC03ARG   73


1e0uD03ARG   73


1pkyA03ARG   73


1pkyB03ARG   73


1pkyC03ARG   73


1pkyD03ARG   73


1a3wA03ARG   91


1a3wB03ARG   91


1a3xA03ARG   91


1a3xB03ARG   91


1pklA03ARG   90


1pklB03ARG   90


1pklC03ARG   90


1pklD03ARG   90


1pklE03ARG   90


1pklF03ARG   90


1pklG03ARG   90


1pklH03ARG   90


1a49A03ARG  119


1a49B03ARG  719


1a49C03ARG 1319


1a49D03ARG 1919


1a49E03ARG 3119


1a49F03ARG 3719


1a49G03ARG 4319


1a49H03ARG 4919


1a5uA03ARG  119


1a5uB03ARG  719


1a5uC03ARG 1319


1a5uD03ARG 1919


1a5uE03ARG 3119


1a5uF03ARG 3719


1a5uG03ARG 4319


1a5uH03ARG 4919


1aqfA03ARG  119


1aqfB03ARG  119


1aqfC03ARG  119


1aqfD03ARG  119


1aqfF03ARG  119


1aqfG03ARG  119


1aqfH03ARG  119


1f3wA03ARG  119


1f3wB03ARG  119


1f3wC03ARG  119


1f3wD03ARG  119


1f3wE03ARG  119


1f3wF03ARG  119


1f3wG03ARG  119


1f3wH03ARG  119


1f3xA03ARG  119


1f3xB03ARG  119


1f3xC03ARG  119


1f3xD03ARG  119


1f3xE03ARG  119


1f3xF03ARG  119


1f3xG03ARG  119


1f3xH03ARG  119


1pknA03ARG  119


1pkmA03ARG  119


1liuA03ARG  163


1liuB03ARG  163


1liuC03ARG  163


1liuD03ARG  163


1liwA03ARG  163


1liwB03ARG  163


1liwC03ARG  163


1liwD03ARG  163


1lixA03ARG  163


1lixB03ARG  163


1lixC03ARG  163


1lixD03ARG  163


1liyA03ARG  163


1liyB03ARG  163


1liyC03ARG  163


1liyD03ARG  163


1t5aA03ARG  120


1t5aB03ARG  120


1t5aC03ARG  120


1t5aD03ARG  120


1zjhA03ARG  119



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Fig.4, Fig.12, p.204
[4]Fig.3, p.629
[8]Scheme II
[10]Fig.5, p.478-480
[13]Fig.7
[28]p.731-734, p.737
[33]

[36]p.6253-6254
[39]p.201-204
[40]p.9142-9144
[41]p.623-624
[52]

[53]Fig.1, p.9423-9424

references
[1]
PubMed ID4522427
JournalAnn N Y Acad Sci
Year1973
Volume222
Pages192-210
AuthorsMildvan AS, Nowak T, Fung CH
TitleNuclear relaxation studies of the role of the divalent cation in the mechanism of pyruvate kinase and enolase: inner sphere and second sphere complexes.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (6 ANGSTROMS)
Medline ID76048760
PubMed ID1185780
JournalJ Mol Biol
Year1975
Volume95
Pages213-25
AuthorsStammers DK, Muirhead H
TitleThree-dimensional structure of cat muscle pyruvate kinase at 6 Angstrom resolution.
Related Swiss-protP11979
[3]
CommentsX-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS)
Medline ID77209973
PubMed ID875020
JournalJ Mol Biol
Year1977
Volume112
Pages309-16
AuthorsStammers DK, Muirhead H
TitleThree-dimensional structure of cat muscle pyruvate kinase at 3-1 A resolution.
Related Swiss-protP11979
[4]
PubMed ID625331
JournalNature
Year1978
Volume271
Pages626-30
AuthorsLevine M, Muirhead H, Stammers DK, Stuart DI
TitleStructure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID80140448
PubMed ID537059
JournalJ Mol Biol
Year1979
Volume134
Pages109-42
AuthorsStuart DI, Levine M, Muirhead H, Stammers DK
TitleCrystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A.
Related Swiss-protP11979
[6]
PubMed ID7274544
JournalBiochem Soc Trans
Year1981
Volume9
Pages212-3
AuthorsMuirhead H, Grant JP, Lawton MA, Midwinter CA, Nocton JC, Stuart DI
TitleThe structure and function of pyruvate kinase.
[7]
PubMed ID6723988
JournalFEBS Lett
Year1984
Volume171
Pages293-6
AuthorsHoar CG, Nicoll GW, Schiltz E, Schmitt W, Bloxham DP, Byford MF, Dunbar B, Fothergill LA
TitleMuscle and liver pyruvate kinases are closely related: amino acid sequence comparisons.
[8]
PubMed ID3910092
JournalBiochemistry
Year1985
Volume24
Pages6163-9
AuthorsHoving H, Crysell B, Leadlay PF
TitleFluorine NMR studies on stereochemical aspects of reactions catalyzed by transcarboxylase, pyruvate kinase, and enzyme I.
[9]
PubMed ID2997192
JournalJ Biol Chem
Year1985
Volume260
Pages14060-9
AuthorsVan Divender JM, Grisham CM
Title7Li, 31P, and 1H NMR studies of interactions between ATP, monovalent cations, and divalent cation sites on rabbit muscle pyruvate kinase.
[10]
PubMed ID3519210
JournalEMBO J
Year1986
Volume5
Pages475-81
AuthorsMuirhead H, Clayden DA, Barford D, Lorimer CG, Fothergill-Gilmore LA, Schiltz E, Schmitt W
TitleThe structure of cat muscle pyruvate kinase.
[11]
PubMed ID3082867
JournalJ Biol Chem
Year1986
Volume261
Pages4499-503
AuthorsDeCamp DL, Colman RF
TitleIdentification of tyrosine and lysine peptides labeled by 5'-p-fluorosulfonylbenzoyl adenosine in the active site of pyruvate kinase.
[12]
PubMed ID3691955
JournalBiochem Soc Trans
Year1987
Volume15
Pages996-9
AuthorsMuirhead H, Clayden DA, Cuffe SP, Davies C
TitleCrystallographic studies on the structure and catalytic activity of pyruvate kinase from skeletal muscle.
[13]
PubMed ID3040085
JournalBiochemistry
Year1987
Volume26
Pages2243-50
AuthorsLodato DT, Reed GH
TitleStructure of the oxalate-ATP complex with pyruvate kinase: ATP as a bridging ligand for the two divalent cations.
[14]
PubMed ID3498511
JournalBiochemistry
Year1987
Volume26
Pages3487-93
AuthorsRosevear PR, Fox TL, Mildvan AS
TitleNuclear Overhauser effect studies of the conformations of MgATP bound to the active and secondary sites of muscle pyruvate kinase.
[15]
PubMed ID3143610
JournalInt J Biochem
Year1988
Volume20
Pages1001-8
AuthorsImarai M, Hinrichsen P, Bazaes S, Wilkens M, Eyzaguirre J
TitleYeast pyruvate kinase: essential lysine residues in the active site.
[16]
PubMed ID3343233
JournalJ Biol Chem
Year1988
Volume263
Pages2794-801
AuthorsConsler TG, Uberbacher EC, Bunick GJ, Liebman MN, Lee JC
TitleDomain interaction in rabbit muscle pyruvate kinase. II. Small angle neutron scattering and computer simulation.
[17]
PubMed ID3343233
JournalJ Biol Chem
Year1988
Volume263
Pages2794-801
AuthorsConsler TG, Uberbacher EC, Bunick GJ, Liebman MN, Lee JC
TitleDomain interaction in rabbit muscle pyruvate kinase. II. Small angle neutron scattering and computer simulation.
[18]
PubMed ID3374614
JournalNature
Year1988
Volume333
Pages683-6
AuthorsLebioda L, Stec B
TitleCrystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor.
[19]
PubMed ID2489027
JournalJ Biol Chem
Year1989
Volume264
Pages8430-41
AuthorsDeCamp DL, Colman RF
Title2-[(4-Bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 5'-diphosphate. A new fluorescent affinity label of a tyrosyl residue in the active site of rabbit muscle pyruvate kinase.
[20]
PubMed ID2334678
JournalBiochemistry
Year1990
Volume29
Pages2495-501
AuthorsVollmer SH, Colman RF
TitleCysteinyl peptides of rabbit muscle pyruvate kinase labeled by the affinity label 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5'-triphosphate.
[21]
PubMed ID1658780
JournalProteins
Year1991
Volume11
Pages153-7
AuthorsSchmidt-Base K, Buchbinder JL, Reed GH, Rayment I
TitleCrystallization and preliminary analysis of enzyme-substrate complexes of pyruvate kinase from rabbit muscle.
[22]
PubMed ID1396575
JournalEMBO J
Year1992
Volume11
Pages3811-4
AuthorsMurcott TH, Gutfreund H, Muirhead H
TitleThe cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase.
[23]
PubMed ID1555604
JournalEur J Biochem
Year1992
Volume205
Pages59-69
AuthorsLandy SB, Ray BD, Plateau P, Lipkowitz KB, Rao BD
TitleConformation of MgATP bound to nucleotidyl and phosphoryl transfer enzymes 1H-transferred NOE measurements on complexes of methionyl tRNA synthetase and pyruvate kinase.
[24]
PubMed ID1304366
JournalProtein Sci
Year1992
Volume1
Pages678-87
AuthorsVollmer SH, Colman RF
TitleCysteinyl peptides labeled by dibromobutanedione in reaction with rabbit muscle pyruvate kinase.
[25]
PubMed ID8260493
JournalBiochemistry
Year1993
Volume32
Pages14111-6
AuthorsBuchbinder JL, Baraniak J, Frey PA, Reed GH
TitleStereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase.
[26]
PubMed ID8204612
JournalBiochemistry
Year1994
Volume33
Pages6784-91
AuthorsJarori GK, Murali N, Rao BD
TitleTwo-dimensional transferred nuclear Overhauser effect spectroscopy study of the confirmation of MgATP bound at the active and ancillary sites of rabbit muscle pyruvate kinase.
[27]
PubMed ID8193145
JournalBiochemistry
Year1994
Volume33
Pages6301-9
AuthorsLarsen TM, Laughlin LT, Holden HM, Rayment I, Reed GH
TitleStructure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate.
[28]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID96000862
PubMed ID8591049
JournalStructure
Year1995
Volume3
Pages729-41
AuthorsMattevi A, Valentini G, Rizzi M, Speranza ML, Bolognesi M, Coda A
TitleCrystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition.
Related PDB1pky
Related Swiss-protP0AD61
[29]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
JournalActa Crystallogr D Biol Crystallogr
Year1996
Volume52
Pages499-504
AuthorsAllen SC, Muirhead H
TitleRefined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A.
Related PDB1pkm
Related Swiss-protP11979
[30]
PubMed ID8682196
JournalFEBS Lett
Year1996
Volume389
Pages15-9
AuthorsMattevi A, Bolognesi M, Valentini G
TitleThe allosteric regulation of pyruvate kinase.
[31]
PubMed ID8626426
JournalJ Biol Chem
Year1996
Volume271
Pages6313-21
AuthorsCheng X, Friesen RH, Lee JC
TitleEffects of conserved residues on the regulation of rabbit muscle pyruvate kinase.
[32]
PubMed ID9010934
JournalProtein Eng
Year1996
Volume9
Pages1203-10
AuthorsCollins RA, Kelly SM, Price NC, Fothergill-Gilmore LA, Muirhead H
TitleLigand-induced conformational changes in wild-type and mutant yeast pyruvate kinase.
[33]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID97452476
PubMed ID9308890
JournalArch Biochem Biophys
Year1997
Volume345
Pages199-206
AuthorsLarsen TM, Benning MM, Wesenberg GE, Rayment I, Reed GH
TitleLigand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution.
Related PDB1aqf,1pkn
Related Swiss-protP11974
[34]
PubMed ID9434737
JournalArch Biochem Biophys
Year1997
Volume348
Pages262-7
AuthorsLaughlin LT, Reed GH
TitleThe monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117.
[35]
PubMed ID9799487
JournalBiochemistry
Year1998
Volume37
Pages15266-76
AuthorsFriesen RH, Castellani RJ, Lee JC, Braun W
TitleAllostery in rabbit pyruvate kinase: development of a strategy to elucidate the mechanism.
[36]
CommentsX-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS)
Medline ID98241346
PubMed ID9572839
JournalBiochemistry
Year1998
Volume37
Pages6247-55
AuthorsLarsen TM, Benning MM, Rayment I, Reed GH
TitleStructure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel.
Related PDB1a49,1a5u
Related Swiss-protP11974
[37]
PubMed ID9578583
JournalBiochemistry
Year1998
Volume37
Pages6967-74
AuthorsLoria JP, Nowak T
TitleConformational changes in yeast pyruvate kinase studied by 205Tl+ NMR.
[38]
PubMed ID9500921
JournalJ Mol Biol
Year1998
Volume276
Pages839-51
AuthorsLovell SC, Mullick AH, Muirhead H
TitleCooperativity in Bacillus stearothermophilus pyruvate kinase.
[39]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
Medline ID98179936
PubMed ID9519410
JournalStructure
Year1998
Volume6
Pages195-210
AuthorsJurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL
TitleThe allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate.
Related PDB1a3w,1a3x
Related Swiss-protP00549
[40]
PubMed ID10413488
JournalBiochemistry
Year1999
Volume38
Pages9137-45
AuthorsBollenbach TJ, Mesecar AD, Nowak T
TitleRole of lysine 240 in the mechanism of yeast pyruvate kinase catalysis.
[41]
CommentsX-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS)
Medline ID99380407
PubMed ID10448041
JournalJ Mol Biol
Year1999
Volume291
Pages615-35
AuthorsRigden DJ, Phillips SE, Michels PA, Fothergill-Gilmore LA
TitleThe structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity.
Related PDB1pkl
Related Swiss-protQ27686
[42]
PubMed ID11019825
JournalArch Biochem Biophys
Year2000
Volume381
Pages99-110
AuthorsEdwin F, Jagannadham MV
TitleAnion-induced folding of rabbit muscle pyruvate kinase: existence of multiple intermediate conformations at low pH.
[43]
PubMed ID10816124
JournalBiochem Soc Trans
Year2000
Volume28
Pages186-90
AuthorsFothergill-Gillmore LA, Rigden DJ, Michels PA, Phillips SE
TitleLeishmania pyruvate kinase: the crystal structure reveals the structural basis of its unique regulatory properties.
[44]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID20309762
PubMed ID10751408
JournalJ Biol Chem
Year2000
Volume275
Pages18145-52
AuthorsValentini G, Chiarelli L, Fortin R, Speranza ML, Galizzi A, Mattevi A
TitleThe allosteric regulation of pyruvate kinase.
Related PDB1e0t,1e0u
Related Swiss-protP0AD61
[45]
PubMed ID11389729
JournalEur J Biochem
Year2001
Volume268
Pages3267-74
AuthorsRamirez-Silva L, Ferreira ST, Nowak T, Tuena de Gomez-Puyou M, Gomez-Puyou A
TitleDimethylsulfoxide promotes K+-independent activity of pyruvate kinase and the acquisition of the active catalytic conformation.
[46]
CommentsX-ray crystallography
PubMed ID11563914
JournalJ Mol Biol
Year2001
Volume312
Pages525-40
AuthorsWooll JO, Friesen RH, White MA, Watowich SJ, Fox RO, Lee JC, Czerwinski EW
TitleStructural and functional linkages between subunit interfaces in mammalian pyruvate kinase.
Related PDB1f3w,1f3x
[47]
PubMed ID11747307
JournalArch Biochem Biophys
Year2002
Volume397
Pages28-39
AuthorsFenton AW, Blair JB
TitleKinetic and allosteric consequences of mutations in the subunit and domain interfaces and the allosteric site of yeast pyruvate kinase.
[48]
PubMed ID11913971
JournalArch Biochem Biophys
Year2002
Volume400
Pages54-62
AuthorsPlaxton WC, Smith CR, Knowles VL
TitleMolecular and regulatory properties of leucoplast pyruvate kinase from Brassica napus (rapeseed) suspension cells.
[49]
PubMed ID11960989
JournalJ Biol Chem
Year2002
Volume277
Pages23807-14
AuthorsValentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A
TitleStructure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.
Related PDB1liu,1liw,1lix,1liy
[50]
PubMed ID12504250
JournalBiophys Chem
Year2003
Volume103
Pages1-11
AuthorsYu S, Lee LL, Lee JC
TitleEffects of metabolites on the structural dynamics of rabbit muscle pyruvate kinase.
[51]
PubMed ID12882975
JournalJ Biol Chem
Year2003
Volume278
Pages40943-52
AuthorsSusan-Resiga D, Nowak T
TitleMonitoring active site alterations upon mutation of yeast pyruvate kinase using 205Tl+ NMR.
[52]
PubMed ID15568816
JournalBiochemistry
Year2004
Volume43
Pages15230-45
AuthorsSusan-Resiga D, Nowak T
TitleProton donor in yeast pyruvate kinase: chemical and kinetic properties of the active site Thr 298 to Cys mutant.
[53]
PubMed ID15996096
JournalBiochemistry
Year2005
Volume44
Pages9417-29
AuthorsDombrauckas JD, Santarsiero BD, Mesecar AD
TitleStructural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis.
Related PDB1t5a

comments
This enzyme binds a potassium ion and two magnesium ions as cofactors. The first magnesium ion is bound to usbtrate, phosphoenolpyruvate, and acidic residues, whereas the second magnesium ion is bound to phosphate groups of the second substrate, ADP, without any interaction with protein residues. Thus, the second magnesium gets bound to the enzyme along with ADP binding. The potassium ion is bound to the transferred group, phosphate group of phosphoenolpyruvate.
This enzyme catalyzes two reactions, firstly phoshoryl transfer and secondly isomerization, as follows (see [36], [39], [40] & [52]):
(A) Transfer of phosphate group from phosphenolpyruvate to ADP:
(A1) The negative charge of the acceptor group, the beta-phosphate of ADP, is stabilized by the second magnesium ion along with Arg119 (of 1a49;PDB). The negative charge of the transferred group is stabilized by the potassium ion and the two magnesium ion, along with Arg72, Lys269 and Arg119. The leaving oxygen atom of phosphoenolpyruvate is stabilized by the first magnesium ion and Lys269.
(A2) The acceptor group, makes a nucleophilic attack on the transferred group, phosphate group of phosphoenolpyruvate, forming enolate intermediate. (This reaction seems associative (or SN2-like), according to the literature [39]).
(B) Isomerization; Shift of double-bond (from C=C-O to C-C=O):
(B1) The first magnesium ion binds the enolate oxygen atom of the intermediate, and stabilizes the negative charge on it. Lys269 also may stabilize it.
(B2) A general acid must protonate the C3 atom (sp2 carbon atom) of the enolate intermediate, changing it to the methyl group (sp3 carbon). Initially, Lys269 was thought to be the general acid (see [10]). However, according to the more recent literature [36], a conserved acidic residue, Glu363, act as a general acid to protonate the sp2 carbon of the intermediate, through water molecules, Ser361 and Thr327. (The carbon atom interacts with a water molecule, which in turn interacts with Thr327. Thr327 interacts with Ser361 through a water, and Ser361 interacts with Glu363 through a water)

createdupdated
2004-03-252009-02-26


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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