EC |
2.3.1.204 |
Accepted name: |
octanoyl-[GcvH]:protein N-octanoyltransferase |
Reaction: |
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] = glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine |
Glossary: |
GcvH = glycine cleavage system H] |
Other name(s): |
LipL; octanoyl-[GcvH]:E2 amidotransferase; ywfL (gene name) |
Systematic name: |
[glycine cleavage system H]-N6-octanoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine octanoyltransferase |
Comments: |
In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the
amidotransfer of the octanoyl moiety from [glycine cleavage system H]-N6-octanoyl-L-lysine (i.e. octanoyl-GcvH) to the E2 subunit (dihydrolipoamide acetyltransferase) of pyruvate dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
References: |
1. |
Christensen, Q.H., Martin, N., Mansilla, M.C., de Mendoza, D. and Cronan, J.E. A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis. Mol. Microbiol. 80 (2011) 350–363. [DOI] [PMID: 21338421] |
2. |
Martin, N., Christensen, Q.H., Mansilla, M.C., Cronan, J.E. and de Mendoza, D. A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis. Mol. Microbiol. 80 (2011) 335–349. [DOI] [PMID: 21338420] |
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[EC 2.3.1.204 created 2012] |
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