ID: | 4.1.1.31 | ||||||||||||||||||||||
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Description: | Phosphoenolpyruvate carboxylase. | ||||||||||||||||||||||
Alternative Name: |
Phosphoenolpyruvic carboxylase. PEPCase. PEP carboxylase. | ||||||||||||||||||||||
Prosite: | PDOC00330; | ||||||||||||||||||||||
PDB: |
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Cath: | 1.20.1440.90; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 |
Title | Authors | Date | PubMed ID |
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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 K | 1997 Dec | 9522466 |
Site-directed mutagenesis of Lys600 in phosphoenolpyruvate carboxylase of Flaveria trinervia: its roles in catalytic and regulatory functions. | Gao Y, Woo KC | 1995 Nov 13 | 7498490 |
Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase. | Yano M, Terada K, Umiji K, Izui K | 1995 Jun | 7490260 |
Physiological implications of the kinetics of maize leaf phosphoenolpyruvate carboxylase. | Tovar-Méndez A, Mújica-Jiménez C, Muñoz-Clares RA | 2000 May | 10806233 |