ENZYME entry: EC 188.8.131.52
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|S-adenosyl-L-methionine + L-tryptophan <=> S-adenosyl-L-homocysteine + L-2-methyltryptophan|
- The enzyme, characterized from the bacterium Streptomyces laurentii,
is involved in thiostrepton biosynthesis.
- It is a radical SAM enzyme that contains a [4Fe-4S] center and a
- The enzyme first transfers the methyl group from SAM to the bound
cobalamin, followed by transfer from methylcobalamin to L-tryptophan,
resulting in retention of the original methyl group configuration.
- The second transfer is likely to involve a CH(3) radical species
formed from methylcobalamin by the concerted action of a partially
ligated radical SAM [4Fe-4S](2+/1+) center.
|PRIAM enzyme-specific profiles||184.108.40.206|
|KEGG Ligand Database for Enzyme Nomenclature||220.127.116.11|
|IUBMB Enzyme Nomenclature||18.104.22.168|
|MEDLINE||Find literature relating to 22.214.171.124|
|Rhea expert-curated reactions||126.96.36.199|
entries corresponding to 2.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.-.-
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