KEGG   ENZYME: 1.3.99.36Help
Entry
EC 1.3.99.36                Enzyme                                 

Name
cypemycin cysteine dehydrogenase (decarboxylating);
cypemycin decarboxylase;
CypD
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With unknown physiological acceptors
BRITE hierarchy
Sysname
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys:acceptor oxidoreductase (decarboxylating, cyclizing)
Reaction(IUBMB)
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor = C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor
Substrate
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys;
acceptor [CPD:C00028]
Product
C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide;
CO2 [CPD:C00011];
H2S [CPD:C00283];
reduced acceptor [CPD:C00030]
Comment
Cypemycin, isolated from the bacterium Streptomyces sp. OH-4156, is a peptide antibiotic, member of the linaridins, a class of posttranslationally modified ribosomally synthesized peptides. The enzyme decarboxylates and reduces the C-terminal L-cysteine residue, producing a reactive ethenethiol group that reacts with a dethiolated cysteine upstream to form an aminovinyl-methyl-cysteine loop that is important for the antibiotic activity of the mature peptide.
History
EC 1.3.99.36 created 2014
Reference
1  [PMID:20805503]
  Authors
Claesen J, Bibb M
  Title
Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 107 (2010) 16297-302.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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