Enzyme

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     6. Ligases
        6.4 Forming carbon-carbon bonds
            6.4.1 Ligases that form carbon-carbon bonds (only sub-subclass identified to date)
ID:6.4.1.1
Description:Pyruvate carboxylase.
Alternative Name: Pyruvic carboxylase.
Prosite: PDOC50991; PDOC50979; PDOC50975; PDOC00676; PDOC00167;
PDB:
PDBScop
Cath: 1.10.10.2790; 1.10.10.60; 1.10.287.160; 1.10.287.1600; 1.10.472.90; 3.10.600.10; 3.20.20.70; 3.30.1490.20; 3.30.470.130; 3.30.470.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 6.4.1.1
BRENDA Enzyme Link: BRENDA 6.4.1.1
KEGG Enzyme Link: KEGG6.4.1.1
BioCyc Enzyme Link: BioCyc 6.4.1.1
ExPASy Enzyme Link: ExPASy6.4.1.1
EC2PDB Enzyme Link: EC2PDB 6.4.1.1
ExplorEnz Enzyme Link: ExplorEnz 6.4.1.1
PRIAM enzyme-specific profiles Link: PRIAM 6.4.1.1
IntEnz Enzyme Link: IntEnz 6.4.1.1
MEDLINE Enzyme Link: MEDLINE 6.4.1.1
MSA:

6.4.1.1;

Phylogenetic Tree:

6.4.1.1;

Uniprot:
M-CSA:
RHEA:20844 ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate
RULE(radius=1) [*:1]-[CH3;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:1]-[CH2;+0:2]-[C;H0;+0:4](=[*:3])-[*:5].[*:12]-[OH;+0:11].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The structure and the mechanism of action of pyruvate carboxylase.Attwood PV1995 Mar7780827
Induction of erythroid differentiation in Friend leukemia cells by bromodeoxyuridine.Adesnik M, Snitkin H1978 Jun649667
Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli.Zeczycki TN, St Maurice M, Jitrapakdee S, Wallace JC, Attwood PV, Cleland WW2009 May 2619341298
Structure, mechanism and regulation of pyruvate carboxylase.Jitrapakdee S, St Maurice M, Rayment I, Cleland WW, Wallace JC, Attwood PV2008 Aug 118613815
Insights into the mechanism and regulation of pyruvate carboxylase by characterisation of a biotin-deficient mutant of the Bacillus thermodenitrificans enzyme.Adina-Zada A, Jitrapakdee S, Surinya KH, McIldowie MJ, Piggott MJ, Cleland WW, Wallace JC, Attwood PV200818272421