Mersacidin decarboxylase

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mersacidin decarboxylase
1p3y.jpg
Mersacidin decarboxylase homododekamer, Bacillus sp.
Identifiers
EC number4.1.1..
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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, D.G.; Altena, K.; Bierbaum, G.; Kupke, T. (2002). "The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction involved in formation of the peptidoglycan biosynthesis inhibitor mersacidin". J. Bacteriol. 184: 1234–1243. PMID 11844751.