KEGG   ENZYME: 2.1.1.106Help
Entry
EC 2.1.1.106                Enzyme                                 

Name
tryptophan 2-C-methyltransferase;
tsrM (gene name);
tryptophan 2-methyltransferase;
S-adenosylmethionine:tryptophan 2-methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:L-tryptophan 2-C-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + L-tryptophan = S-adenosyl-L-homocysteine + L-2-methyltryptophan [RN:R08547]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
L-tryptophan [CPD:C00078]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
L-2-methyltryptophan [CPD:C16831]
Comment
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 cobalamin cofactor. 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 CH3 radical species formed from methylcobalamin by the concerted action of a partially ligated radical SAM [4Fe-4S]2+/1+ center.
History
EC 2.1.1.106 created 1992
Reference
1  [PMID:2321967]
  Authors
Frenzel T, Zhou P, Floss HG.
  Title
Formation of 2-methyltryptophan in the biosynthesis of thiostrepton: isolation of S-adenosylmethionine:tryptophan 2-methyltransferase.
  Journal
Arch. Biochem. Biophys. 278 (1990) 35-40.
Reference
2  [PMID:23064318]
  Authors
Pierre S, Guillot A, Benjdia A, Sandstrom C, Langella P, Berteau O
  Title
Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes.
  Journal
Nat. Chem. Biol. 8 (2012) 957-9.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
126626-83-3

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