Octanoyl-(GcvH):protein N-octanoyltransferase

Summary

Octanoyl-(GcvH):protein N-octanoyltransferase (EC 2.3.1.204, LIPL, octanoyl-[GcvH]:E2 amidotransferase, YWFL (gene)) is an enzyme with systematic name (glycine cleavage system H)-N6-octanoyl-L-lysine:(lipoyl-carrier protein)-N6-L-lysine octanoyltransferase.[1][2] This enzyme catalyses the following chemical reaction

Octanoyl-(GcvH):protein N-octanoyltransferase
Identifiers
EC no.2.3.1.204
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
[glycine cleavage system H]-N6-octanoyl-L-lysine + [lipoyl-carrier protein] glycine cleavage system H + [lipoyl-carrier protein]-N6-octanoyl-L-lysine

This enzyme is purified from the bacterium Bacillus subtilis.

References edit

  1. ^ Christensen QH, Martin N, Mansilla MC, de Mendoza D, Cronan JE (April 2011). "A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis". Molecular Microbiology. 80 (2): 350–63. doi:10.1111/j.1365-2958.2011.07598.x. PMC 3088481. PMID 21338421.
  2. ^ Martin N, Christensen QH, Mansilla MC, Cronan JE, de Mendoza D (April 2011). "A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis". Molecular Microbiology. 80 (2): 335–49. doi:10.1111/j.1365-2958.2011.07597.x. PMC 3086205. PMID 21338420.

External links edit