EC number:4.1.1.71

Enzyme

Download
EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.71
Description:2-oxoglutarate decarboxylase.
Alternative Name: Alpha-ketoglutarate decarboxylase.
2-oxoglutarate carboxy-lyase.
Cath: 1.10.287.1150; 3.40.50.970; 3.40.50.11610; 3.40.50.12470;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

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.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.71
BRENDA Enzyme Link: BRENDA 4.1.1.71
KEGG Enzyme Link: KEGG4.1.1.71
BioCyc Enzyme Link: BioCyc 4.1.1.71
ExPASy Enzyme Link: ExPASy4.1.1.71
EC2PDB Enzyme Link: EC2PDB 4.1.1.71
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.71
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.71
IntEnz Enzyme Link: IntEnz 4.1.1.71
MEDLINE Enzyme Link: MEDLINE 4.1.1.71

EC number:4.1.1.71

MSA:

4.1.1.71;
Phylogenetic Tree:

4.1.1.71;
Uniprot:
M-CSA:
RHEA:10524 2-oxoglutarate + H(+) = CO2 + succinate semialdehyde
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[C;H0;+0:4](=[*:5])-[*:6].[H+;H0:7]>>[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[*:5]=[CH;+0:4]-[*:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Functional plasticity and allosteric regulation of α-ketoglutarate decarboxylase in central mycobacterial metabolism.Wagner T, Bellinzoni M, Wehenkel A, O'Hare HM, Alzari PM2011 Aug 2621867916