Jump to content

Mersacidin decarboxylase

From Wikipedia, the free encyclopedia
mersacidin decarboxylase
Mersacidin decarboxylase homododekamer, Bacillus sp.
Identifiers
EC no.4.1.1..
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Mersacidin decarboxylase EC 4.1.1.. MrsD is an enzyme that catalyzes the oxidative decarboxylation of the C-terminal cysteine residue of mersacidin to an aminoenethiol residue,[1] intermediate as the first step in the formation of the unusual amino acid S-[(Z)-2-aminovinyl]-methyl-D-cysteine with coenzyme FAD

References

[edit]
  1. ^ Majer F, Schmid DG, Altena K, Bierbaum G, Kupke T (March 2002). "The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction involved in formation of the peptidoglycan biosynthesis inhibitor mersacidin". Journal of Bacteriology. 184 (5): 1234–43. doi:10.1128/jb.184.5.1234-1243.2002. PMC 134850. PMID 11844751.