| 词条 | Mersacidin decarboxylase |
| 释义 |
| Name = mersacidin decarboxylase | EC_number = 4.1.1.. | CAS_number = | IUBMB_EC_number = 4/1/1/.. | GO_code = | image = 1p3y.jpg | width = 270 | caption = Mersacidin decarboxylase homododekamer, Bacillus sp. }} Mersacidin decarboxylase {{EC number|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 References1. ^{{cite journal | title = The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction involved in formation of the peptidoglycan biosynthesis inhibitor mersacidin. |author1 = Majer, F. |author2 = Schmid, D.G. |author3 = Altena, K. |author4 = Bierbaum, G. |author5 = Kupke, T. |journal = J. Bacteriol. |year = 2002 |volume = 184 |pages = 1234–1243 |pmid= 11844751 }} {{Carbon-carbon lyases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}} 2 : EC 4.1.1|Bacterial proteins |
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