Mersacidin decarboxylase

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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
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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.