T00084
type: Enzyme
active site residues resources: Identification of reactive conserved histidines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae.
active site residues resources: Structure and mechanism of phosphoenolpyruvate carboxykinase.
active site residues resources: Characterization of the oxaloacetate decarboxylase and pyruvate kinase-like activities of Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinases.
active site residues resources: Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: theoretical and experimental study of the effect of glutamic acid 284 on the protonation state of lysine 213.
active site residues resources: Thermal stability of phosphoenolpyruvate carboxykinases from Escherichia coli, Trypanosoma brucei, and Saccharomyces cerevisiae.
active site residues resources: Crystal structure of Anaerobiospirillum succiniciproducens PEP carboxykinase reveals an important active site loop.
cath: Phosphoenolpyruvate Carboxykinase; domain 1
cath: Phosphoenolpyruvate Carboxykinase; domain 2
cath: Phosphoenolpyruvate Carboxykinase; domain 3
csa: 1aq2
ec: https://purl.uniprot.org/enzyme/4.1.1.49
kegg cofactor: Magnesium
kegg cofactor: Divalent metal
kegg enzyme: phosphoenolpyruvate carboxykinase (ATP)
kegg intermediate: Enolpyruvate
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Citrate cycle (TCA cycle)
kegg pathway: Pyruvate metabolism
kegg pathway: Carbon fixation in photosynthetic organisms
kegg product: ADP
kegg product: Phosphoenolpyruvate
kegg product: CO2
kegg substrate: ATP
kegg substrate: Oxaloacetate
macie: M0051
pdb: 1aq2A01
pdb: 1aylA01
pdb: 1oenA01
pdb: 1k3cA01
pdb: 1k3dA01
pdb: 1os1A01
pdb: 1yvyA01
pdb: 1yvyB01
pdb: 1ylhA01
pdb: 1wg9A01
pdb: 1wg9B01
pdb: 1ii2A01
pdb: 1ii2B01
pdb: 1aq2A02
pdb: 1aylA02
pdb: 1oenA02
pdb: 1k3cA02
pdb: 1k3dA02
pdb: 1os1A02
pdb: 1yvyA02
pdb: 1yvyB02
pdb: 1ylhA02
pdb: 1wg9A02
pdb: 1wg9B02
pdb: 1ii2A02
pdb: 1ii2B02
pdb: 1aq2A03
pdb: 1aylA03
pdb: 1oenA03
pdb: 1k3cA03
pdb: 1k3dA03
pdb: 1os1A03
pdb: 1yvyA03
pdb: 1yvyB03
pdb: 1ylhA03
pdb: 1wg9A03
pdb: 1wg9B03
pdb: 1ii2A03
pdb: 1ii2B03
rlcp: p410
rlcp: p1140
uniprot: P22259
uniprot: O09460
uniprot: Q6W6X5
uniprot: Q5SLL5
uniprot: P51058
references: Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: revised amino acid sequence, site-directed mutagenesis, and microenvironment characteristics of cysteines 365 and 458.
references: Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold.
references: Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase.
references: Identification of reactive conserved histidines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae.
references: Structure and mechanism of phosphoenolpyruvate carboxykinase.
references: Mg(2+)-Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions.
references: The strongly conserved lysine 256 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase is essential for phosphoryl transfer.
references: Characterization of the oxaloacetate decarboxylase and pyruvate kinase-like activities of Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinases.

Phosphoenolpyruvate Carboxykinase; domain 2
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/2.170.8.10

Phosphoenolpyruvate Carboxykinase; domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.449.10

Phosphoenolpyruvate Carboxykinase; domain 3
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.90.228.20

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Citrate cycle (TCA cycle)
type: KeggPathway
references: KEGG:MAP00020

Pyruvate metabolism
type: KeggPathway
references: KEGG:MAP00620

Carbon fixation in photosynthetic organisms
type: KeggPathway
references: KEGG:MAP00710

Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: revised amino acid sequence, site-directed mutagenesis, and microenvironment characteristics of cysteines 365 and 458.
type: BibliographicResource
authors:
  item: Krautwurst H
  item: Encinas MV
  item: Marcus F
  item: Latshaw SP
  item: Kemp RG
  item: Frey PA
  item: Cardemil E
journal: Biochemistry
pages: 6382-8
published year: 1995
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/7756267

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00084#10
type: BibliographicResource
title: Gene- and activation-specific mechanisms for insulin inhibition of basal and glucocorticoid-induced insulin-like growth factor binding protein-1 and phosphoenolpyruvate carboxykinase transcription. Roles of forkhead and insulin response sequences.
authors:
  item: Yeagley D
  item: Guo S
  item: Unterman T
  item: Quinn PG
journal: J Biol Chem
pages: 33705-10
published year: 2001
volume: 276
references: http://www.ncbi.nlm.nih.gov/pubmed/11445561

The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3).
type: BibliographicResource
authors:
  item: Sudom AM
  item: Prasad L
  item: Goldie H
  item: Delbaere LT
journal: J Mol Biol
pages: 83-92
published year: 2001
volume: 314
references: http://www.ncbi.nlm.nih.gov/pubmed/11724534
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 A resolution.
type: BibliographicResource
authors:
  item: Trapani S
  item: Linss J
  item: Goldenberg S
  item: Fischer H
  item: Craievich AF
  item: Oliva G
journal: J Mol Biol
pages: 1059-72
published year: 2001
volume: 313
references: http://www.ncbi.nlm.nih.gov/pubmed/11700062
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Lysine 213 and histidine 233 participate in Mn(II) binding and catalysis in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase.
type: BibliographicResource
authors:
  item: Krautwurst H
  item: Roschzttardtz H
  item: Bazaes S
  item: Gonzalez-Nilo FD
  item: Nowak T
  item: Cardemil E
journal: Biochemistry
pages: 12763-70
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/12379119

Evolutionary relationship between the bacterial HPr kinase and the ubiquitous PEP-carboxykinase: expanding the P-loop nucleotidyl transferase superfamily.
type: BibliographicResource
authors:
  item: Russell RB
  item: Marquez JA
  item: Hengstenberg W
  item: Scheffzek K
journal: FEBS Lett
pages: 1-6
published year: 2002
volume: 517
references: http://www.ncbi.nlm.nih.gov/pubmed/12062398

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00084#16
type: BibliographicResource
title: Urea-induced unfolding studies of free- and ligand-bound tetrameric ATP-dependent Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Influence of quaternary structure on protein conformational stability.
authors:
  item: Encinas MV
  item: Gonzalez-Nilo FD
  item: Andreu JM
  item: Alfonso C
  item: Cardemil E
journal: Int J Biochem Cell Biol
pages: 645-56
published year: 2002
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/11943595

Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site.
type: BibliographicResource
authors:
  item: Dunten P
  item: Weber D
  item: Wertheimer SJ
  item: Belunis C
  item: Crowther R
  item: Hollfelder K
  item: Kammlott U
  item: Levin W
  item: Michel H
  item: Ramsey GB
  item: Swain A
journal: J Mol Biol
pages: 257-64
published year: 2002
volume: 316
references: http://www.ncbi.nlm.nih.gov/pubmed/11851336

The effect of active site mutations in the oxaloacetate decarboxylase and pyruvate kinase-like activities of Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinase.
type: BibliographicResource
authors:
  item: Jabalquinto AM
  item: Laivenieks M
  item: Cabezas M
  item: Zeikus JG
  item: Cardemil E
journal: J Protein Chem
pages: 443-5
published year: 2002
volume: 21
references: http://www.ncbi.nlm.nih.gov/pubmed/12523647

X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr.
type: BibliographicResource
authors:
  item: Fieulaine S
  item: Morera S
  item: Poncet S
  item: Mijakovic I
  item: Galinier A
  item: Janin J
  item: Deutscher J
  item: Nessler S
journal: Proc Natl Acad Sci U S A
pages: 13437-41
published year: 2002
volume: 99
references: http://www.ncbi.nlm.nih.gov/pubmed/12359875

Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold.
type: BibliographicResource
authors:
  item: Matte A
  item: Goldie H
  item: Sweet RM
  item: Delbaere LT
journal: J Mol Biol
medline id: 96190956
pages: 126-43
published year: 1996
volume: 256
references: http://www.ncbi.nlm.nih.gov/pubmed/8609605
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P22259
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Mechanisms of activation of phosphoenolpyruvate carboxykinase from Escherichia coli by Ca2+ and of desensitization by trypsin.
type: BibliographicResource
authors:
  item: Sudom A
  item: Walters R
  item: Pastushok L
  item: Goldie D
  item: Prasad L
  item: Delbaere LT
  item: Goldie H
journal: J Bacteriol
pages: 4233-42
published year: 2003
volume: 185
references: http://www.ncbi.nlm.nih.gov/pubmed/12837799
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure/function studies of phosphoryl transfer by phosphoenolpyruvate carboxykinase.
type: BibliographicResource
authors:
  item: Delbaere LT
  item: Sudom AM
  item: Prasad L
  item: Leduc Y
  item: Goldie H
journal: Biochim Biophys Acta
pages: 271-8
published year: 2004
volume: 1697
references: http://www.ncbi.nlm.nih.gov/pubmed/15023367

Structure of PEP carboxykinase from the succinate-producing Actinobacillus succinogenes: a new conserved active-site motif.
type: BibliographicResource
authors:
  item: Leduc YA
  item: Prasad L
  item: Laivenieks M
  item: Zeikus JG
  item: Delbaere LT
journal: Acta Crystallogr D Biol Crystallogr
pages: 903-12
published year: 2005
volume: 61
references: http://www.ncbi.nlm.nih.gov/pubmed/15983413
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase.
type: BibliographicResource
authors:
  item: Tari LW
  item: Matte A
  item: Pugazhenthi U
  item: Goldie H
  item: Delbaere LT
journal: Nat Struct Biol
medline id: 96185447
pages: 355-63
published year: 1996
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/8599762
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P22259
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Mg(2+)-Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions.
type: BibliographicResource
authors:
  item: Tari LW
  item: Matte A
  item: Goldie H
  item: Delbaere LT
journal: Nat Struct Biol
medline id: 98069645
pages: 990-4
published year: 1997
volume: 4
references: http://www.ncbi.nlm.nih.gov/pubmed/9406547
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P22259
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

The strongly conserved lysine 256 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase is essential for phosphoryl transfer.
type: BibliographicResource
authors:
  item: Krautwurst H
  item: Bazaes S
  item: Gonzalez FD
  item: Jabalquinto AM
  item: Frey PA
  item: Cardemil E
journal: Biochemistry
pages: 6295-302
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9572844

Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity.
type: BibliographicResource
authors:
  item: Llanos L
  item: Briones R
  item: Yevenes A
  item: Gonzalez-Nilo FD
  item: Frey PA
  item: Cardemil E
journal: FEBS Lett
pages: 1-5
published year: 2001
volume: 493
references: http://www.ncbi.nlm.nih.gov/pubmed/11277994

Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: theoretical and experimental study of the effect of glutamic acid 284 on the protonation state of lysine 213.
type: BibliographicResource
authors:
  item: Gonzalez-Nilo FD
  item: Krautwurst H
  item: Yevenes A
  item: Cardemil E
  item: Cachau R
journal: Biochim Biophys Acta
pages: 65-71
published year: 2002
volume: 1599
references: http://www.ncbi.nlm.nih.gov/pubmed/12479406

Thermal stability of phosphoenolpyruvate carboxykinases from Escherichia coli, Trypanosoma brucei, and Saccharomyces cerevisiae.
type: BibliographicResource
authors:
  item: Ravanal MC
  item: Goldie H
  item: Cardemil E
journal: J Protein Chem
pages: 311-5
published year: 2003
volume: 22
references: http://www.ncbi.nlm.nih.gov/pubmed/13678294

Crystal structure of Anaerobiospirillum succiniciproducens PEP carboxykinase reveals an important active site loop.
type: BibliographicResource
authors:
  item: Cotelesage JJ
  item: Prasad L
  item: Zeikus JG
  item: Laivenieks M
  item: Delbaere LT
journal: Int J Biochem Cell Biol
pages: 1829-37
published year: 2005
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/15890557
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Identification of reactive conserved histidines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae.
type: BibliographicResource
authors:
  item: Bazaes S
  item: Montecinos L
  item: Krautwurst H
  item: Goldie H
  item: Cardemil E
  item: Jabalquinto AM
journal: Biochim Biophys Acta
pages: 166-74
published year: 1997
volume: 1337
references: http://www.ncbi.nlm.nih.gov/pubmed/9048893

Structure and mechanism of phosphoenolpyruvate carboxykinase.
type: BibliographicResource
authors:
  item: Matte A
  item: Tari LW
  item: Goldie H
  item: Delbaere LT
journal: J Biol Chem
pages: 8105-8
published year: 1997
volume: 272
references: http://www.ncbi.nlm.nih.gov/pubmed/9139042

Characterization of the oxaloacetate decarboxylase and pyruvate kinase-like activities of Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinases.
type: BibliographicResource
authors:
  item: Jabalquinto AM
  item: Laivenieks M
  item: Zeikus JG
  item: Cardemil E
journal: J Protein Chem
pages: 659-64
published year: 1999
volume: 18
references: http://www.ncbi.nlm.nih.gov/pubmed/10609641

1aq2A03
type: Pdb
catalytic residue: LYS 254
cofactor binding residue: HIS 232;ASP 269(2nd metal binding);THR 255(Magnesium binding)
main chain in catalysis: GLY 251
references: 1aq2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aq2

1os1A03
type: Pdb
catalytic residue: LYS 254
cofactor binding residue: HIS 232;ASP 269(2nd metal binding);THR 255(Magnesium binding)
main chain in catalysis: GLY 251
references: 1os1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1os1

1aylA03
type: Pdb
catalytic residue: LYS 254
cofactor binding residue: HIS 232;ASP 269(2nd metal binding);THR 255(Magnesium binding)
main chain in catalysis: GLY 251
references: 1ayl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ayl

1k3cA03
type: Pdb
catalytic residue: LYS 254
cofactor binding residue: HIS 232;ASP 269(2nd metal binding);THR 255(Magnesium binding)
main chain in catalysis: GLY 251
references: 1k3c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3c

1k3dA03
type: Pdb
catalytic residue: LYS 254
cofactor binding residue: HIS 232;ASP 269(2nd metal binding);THR 255(Magnesium binding)
main chain in catalysis: GLY 251
references: 1k3d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3d

1wg9A03
type: Pdb
catalytic residue: LYS 238
cofactor binding residue: HIS 216;ASP 253(2nd metal binding);THR 239(Magnesium binding)
main chain in catalysis: GLY 235
references: 1wg9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wg9

1ylhA03
type: Pdb
catalytic residue: LYS 254
cofactor binding residue: HIS 232;ASP 269(2nd metal binding);THR 255(Magnesium binding)
main chain in catalysis: GLY 251
references: 1ylh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ylh

1aq2A01
type: Pdb
catalytic residue: TYR 207
cofactor binding residue: LYS 213(2nd metal binding)
references: 1aq2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aq2

1aq2A02
type: Pdb
catalytic residue: ARG 333
references: 1aq2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aq2

1aylA01
type: Pdb
catalytic residue: TYR 207
cofactor binding residue: LYS 213(2nd metal binding)
references: 1ayl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ayl

1aylA02
type: Pdb
catalytic residue: ARG 333
references: 1ayl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ayl

1ii2A01
type: Pdb
catalytic residue: TYR 180
cofactor binding residue: LYS 186(2nd metal binding)
references: 1ii2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ii2

1ii2A02
type: Pdb
catalytic residue: ARG 307
references: 1ii2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ii2

1ii2A03
type: Pdb
catalytic residue: LYS 227
cofactor binding residue: HIS 205;ASP 242(2nd metal binding);THR 228(Magnesium binding)
main chain in catalysis: GLY 224
references: 1ii2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ii2

1ii2B01
type: Pdb
catalytic residue: TYR 180
cofactor binding residue: LYS 186(2nd metal binding)
references: 1ii2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ii2

1ii2B02
type: Pdb
catalytic residue: ARG 307
references: 1ii2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ii2

1ii2B03
type: Pdb
catalytic residue: LYS 227
cofactor binding residue: HIS 205;ASP 242(2nd metal binding);THR 228(Magnesium binding)
main chain in catalysis: GLY 224
references: 1ii2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ii2

1k3cA01
type: Pdb
catalytic residue: TYR 207
cofactor binding residue: LYS 213(2nd metal binding)
references: 1k3c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3c

1k3cA02
type: Pdb
catalytic residue: ARG 333
references: 1k3c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3c

1k3dA01
type: Pdb
catalytic residue: TYR 207
cofactor binding residue: LYS 213(2nd metal binding)
references: 1k3d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3d

1k3dA02
type: Pdb
catalytic residue: ARG 333
references: 1k3d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3d

1oenA01
type: Pdb
catalytic residue: TYR 207
cofactor binding residue: LYS 213(2nd metal binding)
references: 1oen
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oen

1oenA02
type: Pdb
catalytic residue: ARG 333
references: 1oen
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oen

1oenA03
type: Pdb
catalytic residue: LYS 254
cofactor binding residue: HIS 232;ASP 269(2nd metal binding);THR 255(Magnesium binding)
main chain in catalysis: GLY 251
references: 1oen
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oen

1os1A01
type: Pdb
catalytic residue: TYR 207
cofactor binding residue: LYS 213(2nd metal binding)
references: 1os1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1os1

1os1A02
type: Pdb
catalytic residue: ARG 333
references: 1os1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1os1

1wg9A01
type: Pdb
catalytic residue: TYR 191
cofactor binding residue: LYS 197(2nd metal binding)
references: 1wg9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wg9

1wg9A02
type: Pdb
catalytic residue: ARG 319
references: 1wg9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wg9

1wg9B01
type: Pdb
catalytic residue: TYR 191
cofactor binding residue: LYS 197(2nd metal binding)
references: 1wg9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wg9

1wg9B02
type: Pdb
catalytic residue: ARG 319
references: 1wg9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wg9

1wg9B03
type: Pdb
catalytic residue: LYS 238
cofactor binding residue: HIS 216;ASP 253(2nd metal binding);THR 239(Magnesium binding)
main chain in catalysis: GLY 235
references: 1wg9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wg9

1ylhA01
type: Pdb
catalytic residue: TYR 207
cofactor binding residue: LYS 213(2nd metal binding)
references: 1ylh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ylh

1ylhA02
type: Pdb
catalytic residue: ARG 333
references: 1ylh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ylh

1yvyA01
type: Pdb
catalytic residue: TYR 200
cofactor binding residue: LYS 206(2nd metal binding)
references: 1yvy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yvy

1yvyA02
type: Pdb
catalytic residue: ARG 327
references: 1yvy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yvy

1yvyA03
type: Pdb
catalytic residue: LYS 248
cofactor binding residue: HIS 225;ASP 263(2nd metal binding);THR 249(Magnesium binding)
main chain in catalysis: GLY 245
references: 1yvy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yvy

1yvyB01
type: Pdb
catalytic residue: TYR 1200
cofactor binding residue: LYS 1206(2nd metal binding)
references: 1yvy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yvy

1yvyB02
type: Pdb
catalytic residue: ARG 1327
references: 1yvy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yvy

1yvyB03
type: Pdb
catalytic residue: LYS 1248
cofactor binding residue: HIS 1225;ASP 1263(2nd metal binding);THR 1249(Magnesium binding)
main chain in catalysis: GLY 1245
references: 1yvy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yvy

Magnesium
type: KeggCofactor
compound type: divalent metal (Ca2+, Mg2+)
references: KEGG:C00305
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ATP
type: KeggSubstrate
compound type: amine group
compound type: nucleotide
references: KEGG:C00002
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Divalent metal
type: KeggCofactor
compound type: divalent metal (Ca2+, Mg2+)
references: KEGG:C02148

ADP
type: KeggProduct
compound type: amine group
compound type: nucleotide
references: KEGG:C00008
references: CHEBI:16761
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

CO2
type: KeggProduct
compound type: others
references: KEGG:C00011
references: CHEBI:16526
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Oxaloacetate
type: KeggSubstrate
compound type: carbohydrate
compound type: carboxyl group
references: KEGG:C00036
references: CHEBI:30744
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Phosphoenolpyruvate
type: KeggProduct
compound type: carboxyl group
compound type: phosphate group/phosphate ion
references: KEGG:C00074
references: CHEBI:44897
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Enolpyruvate
type: KeggIntermediate
references: KEGG:I00001

phosphopyruvate carboxylase (ATP)
type: KeggEnzyme

phosphoenolpyruvate carboxylase
type: KeggEnzyme

phosphoenolpyruvate carboxykinase
type: KeggEnzyme

phosphoenolpyruvate carboxykinase
type: KeggEnzyme

phosphopyruvate carboxykinase (adenosine triphosphate)
type: KeggEnzyme

PEP carboxylase
type: KeggEnzyme

PEP carboxykinase
type: KeggEnzyme

PEPCK (ATP)
type: KeggEnzyme

PEPK
type: KeggEnzyme

PEPCK
type: KeggEnzyme

phosphoenolpyruvic carboxylase
type: KeggEnzyme

phosphoenolpyruvic carboxykinase
type: KeggEnzyme

phosphoenolpyruvate carboxylase (ATP)
type: KeggEnzyme

phosphopyruvate carboxykinase
type: KeggEnzyme

ATP:oxaloacetate carboxy-lyase (transphosphorylating)
type: KeggEnzyme

IntermediateBound
compound: Enolpyruvate
ligand het code: PYR
pdb: 1aq2A01

IntermediateAnalogue
compound: Enolpyruvate
ligand het code: OXL
pdb: 1aylA01

IntermediateBound
compound: Enolpyruvate
ligand het code: PYR
pdb: 1k3cA01

IntermediateBound
compound: Enolpyruvate
ligand het code: PYR
pdb: 1os1A01

IntermediateBound
compound: Enolpyruvate
ligand het code: PYR
pdb: 1ylhA01

TransitionStateAnalogue
ligand het code: ADP-AF3-PYR
pdb: 1k3cA03

TransitionStateAnalogue
ligand het code: ADP-AF3
pdb: 1k3dA03

ReferenceForCatalyticMechanism
reference index: 2
reference section: p.133-135

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.8, p.360-361
reference step: 2

ReferenceForCatalyticMechanism
reference index: 5
reference section: Scheme 2, p.8107-8108
reference step: 2

ReferenceForCatalyticMechanism
reference index: 6
reference section: Fig.3, p.992-994
reference step: 3

ReferenceForCatalyticMechanism
reference index: 7
reference section: p.6300-6301

ReferenceForCatalyticMechanism
reference index: 9
reference section: p.3-5

ReferenceForCatalyticMechanism
reference index: 11
reference section: p.87-89

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.1064-1066

ReferenceForCatalyticMechanism
reference index: 13

ReferenceForCatalyticMechanism
reference index: 14

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig.9, p.4240-4241
reference step: 3

ReferenceForCatalyticMechanism
reference index: 22
reference section: Fig.4. p.275
reference step: 2

ReferenceForCatalyticMechanism
reference index: 23
reference section: Fig.7, p.1835