Enzyme

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     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.31
Description:Phosphoenolpyruvate carboxylase.
Alternative Name: Phosphoenolpyruvic carboxylase.
PEPCase.
PEP carboxylase.
Prosite: PDOC00330;
PDB:
PDBScop
1QB4 8030288; 8042667;
1JQN 8030288; 8042667;
1FIY 8030288; 8042667;
5VYJ
5FDN
 » show all

Cath: 1.20.1440.90;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.31
BRENDA Enzyme Link: BRENDA 4.1.1.31
KEGG Enzyme Link: KEGG4.1.1.31
BioCyc Enzyme Link: BioCyc 4.1.1.31
ExPASy Enzyme Link: ExPASy4.1.1.31
EC2PDB Enzyme Link: EC2PDB 4.1.1.31
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.31
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.31
IntEnz Enzyme Link: IntEnz 4.1.1.31
MEDLINE Enzyme Link: MEDLINE 4.1.1.31
MSA:

4.1.1.31;

Phylogenetic Tree:

4.1.1.31;

Uniprot:
M-CSA:
RHEA:28370 oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[CH2;+0:4]-[C;H0;+0:5](=[*:6])-[*:7].[*:8]-[OH;+0:9]>>[*:8]-[O;H0;+0:9]-[C;H0;+0:2](-[*:1])=[CH2;+0:4].[*:6]=[C;H0;+0:5](-[*:7])-[OH;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Effects of site-directed mutagenesis of conserved Lys606 residue on catalytic and regulatory functions of maize C4-form phosphoenolpyruvate carboxylase.Dong LY, Ueno Y, Hata S, Izui K1997 Dec9522466
Site-directed mutagenesis of Lys600 in phosphoenolpyruvate carboxylase of Flaveria trinervia: its roles in catalytic and regulatory functions.Gao Y, Woo KC1995 Nov 137498490
Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase.Yano M, Terada K, Umiji K, Izui K1995 Jun7490260
Physiological implications of the kinetics of maize leaf phosphoenolpyruvate carboxylase.Tovar-Méndez A, Mújica-Jiménez C, Muñoz-Clares RA2000 May10806233