IUBMB Enzyme Nomenclature

EC 2.3.1.204

Accepted name: lipoyl-[GcvH]:protein N-lipoyltransferase

Reaction: [glycine cleavage system H protein]-N6-dihydrolipoyl-L-lysine + a [lipoyl-carrier protein] = [glycine cleavage system H protein] + a [lipoyl-carrier protein]-N6-dihydrolipoyl-L-lysine

Glossary: glycine cleavage system H protein = GcvH

Other name(s): LipL; octanoyl-[GcvH]:E2 amidotransferase; ywfL (gene name); octanoyl-[GcvH]:protein N-octanoyltransferase; [glycine cleavage system H]-N6-octanoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine octanoyltransferase

Systematic name: [glycine cleavage system H protein]-N6-dihydrolipoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine dihydrolipoyltransferase

Comments: In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the amidotransfer of the dihydrolipoyl moiety from either the H protein of the glycine cleavage system (EC 1.4.1.27) or the E2 component (dihydrolipoamide acetyltransferase) of the 2-oxoglutarate dehydrogenase system (EC 1.2.1.105) to the E2 component of other 2-oxoacid dehydrogenase systems: the pyruvate dehydrogenase system (EC 1.2.1.104), the branched-chain α-keto acid dehydrogenase system (EC 1.2.1.25), and the acetoin dehydrogenase system (EC 2.3.1.190).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:

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. [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. [PMID: 21338420]

3. Rasetto, N.B., Lavatelli, A., Martin, N. and Mansilla, M.C. Unravelling the lipoyl-relay of exogenous lipoate utilization in Bacillus subtilis, Mol. Microbiol. 112 (2019) 302-316. [PMID: 31066113]

4. Cronan, J.E. Lipoic acid attachment to proteins: stimulating new developments. Microbiol. Mol. Biol. Rev. 88 (2024) e0000524. [PMID: 38624243]

[EC 2.3.1.204 created 2012, modified 2025]


Return to EC 2.3.1 home page
Return to EC 2.3 home page
Return to EC 2 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page