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
Orthology
K21551  tryptophan 2-C-methyltransferase
Genes
KSK: KSE_17820
NOA: BKM31_33400
ASE: ACPL_3589
Taxonomy
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 278:35-40 (1990)
DOI:10.1016/0003-9861(90)90227-P
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 8:957-9 (2012)
DOI:10.1038/nchembio.1091
  Sequence
Reference
3  [PMID:26841310]
  Authors
Blaszczyk AJ, Silakov A, Zhang B, Maiocco SJ, Lanz ND, Kelly WL, Elliott SJ, Krebs C, Booker SJ
  Title
Spectroscopic and Electrochemical Characterization of the Iron-Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase.
  Journal
J Am Chem Soc 138:3416-26 (2016)
DOI:10.1021/jacs.5b12592
Reference
4  [PMID:28747433]
  Authors
Blaszczyk AJ, Wang B, Silakov A, Ho JV, Booker SJ
  Title
Efficient methylation of C2 in l-tryptophan by the cobalamin-dependent radical S-adenosylmethionine methylase TsrM requires an unmodified N1 amine.
  Journal
J Biol Chem 292:15456-15467 (2017)
DOI:10.1074/jbc.M117.778548
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.106
IUBMB Enzyme Nomenclature: 2.1.1.106
ExPASy - ENZYME nomenclature database: 2.1.1.106
BRENDA, the Enzyme Database: 2.1.1.106
CAS: 126626-83-3

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