Entry |
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Name |
cypemycin cysteine dehydrogenase (decarboxylating);
cypemycin decarboxylase;
CypD
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Class |
Oxidoreductases;
Acting on the CH-CH group of donors;
With unknown physiological acceptors
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Sysname |
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys:acceptor oxidoreductase (decarboxylating, cyclizing)
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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
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Substrate |
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys;
acceptor [CPD: C00028]
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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]
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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.
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History |
EC 1.3.99.36 created 2014
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Orthology |
K21818 | cypemycin cysteine dehydrogenase (decarboxylating) |
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Genes |
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Reference |
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Authors |
Claesen J, Bibb M |
Title |
Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides. |
Journal |
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Sequence |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 1.3.99.36 |
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