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IUBMB Comments 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.
The taxonomic range for the selected organisms is: Streptomyces laurentii The enzyme appears in selected viruses and cellular organisms
Synonyms
S-adenosylmethionine:tryptophan 2-methyltransferase, thiostrepton A tryptophan methyltransferase, thiostrepton tryptophan methyltransferase, tryptophan 2-methyltransferase, TsrM, TsrT,
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thiostrepton A tryptophan methyltransferase
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thiostrepton tryptophan methyltransferase
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S-adenosylmethionine:tryptophan 2-methyltransferase
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tryptophan 2-methyltransferase
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methyl group transfer
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S-adenosyl-L-methionine:L-tryptophan 2-C-methyltransferase
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.
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S-adenosyl-L-methionine + 3-methylindole
S-adenosyl-L-homocysteine + ?
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?
S-adenosyl-L-methionine + D-tryptophan
S-adenosyl-L-homocysteine + D-2-methyltryptophan
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?
S-adenosyl-L-methionine + L-5-fluoro-tryptophan
S-adenosyl-L-homocysteine + L-5-fluoro-2-methyltryptophan
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?
S-adenosyl-L-methionine + L-5-hydroxy-tryptophan
S-adenosyl-L-homocysteine + L-5-hydroxy-2-methyltryptophan
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?
S-adenosyl-L-methionine + L-5-methyl-tryptophan
S-adenosyl-L-homocysteine + L-2,5-dimethyltryptophan
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?
S-adenosyl-L-methionine + L-tryptophan
S-adenosyl-L-homocysteine + L-2-methyltryptophan
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?
S-adenosyl-L-methionine + melatonin
S-adenosyl-L-homocysteine + ?
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?
S-adenosyl-L-methionine + serotonin
S-adenosyl-L-homocysteine + ?
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S-adenosyl-L-methionine + D,L-tryptophan
S-adenosyl-L-homocysteine + D,L-2-methyltryptophan
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significant slower reaction rate with D-tryptophan
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additional information
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additional information
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no activity with methylcobalamin
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additional information
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TsrM does not catalyse substrate H-atom abstraction but probably exploits a radical-based C-methylation mechanism. TsrM catalyzes methyl transfer to all Trp derivatives tested that are substituted on the indole ring
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S-adenosyl-L-methionine + L-tryptophan
S-adenosyl-L-homocysteine + L-2-methyltryptophan
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?
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5'-deoxyadenosylcobalamin
5'-deoxyadenosylcob(III)alamin may substitute for methylcob(III)alamin, albeit only in the presence of light
methylcobalamin
probable physiological enzyme cofactor methylcob(III)alamin, and cob(II)alamin rather than cob(I)alamin is a key reaction intermediate
methylcobinamide
about 5% of the activity with methylcob(III)alamin
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1-Methyltryptophan
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product inhibition
S-adenosyl-L-homocysteine
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0.12
S-adenosyl-L-methionine
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cell free extract
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0.48
S-adenosyl-L-homocysteine
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0.6
substrate L-5-fluoro-tryptophan, pH 7.5, 25°C
1.2
substrate L-5-hydroxy-tryptophan, pH 7.5, 25°C
1.3
substrate L-5-methyl-tryptophan, pH 7.5, 25°C
3.5
cofactor hydroxycob(III)alamin, in presence of dithiothreitol, pH 7.5, 25°C
3.9
cofactor methylcob(III)alamin, pH 7.5, 25°C
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6.8 - 9
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half-maximal activity at pH 6.8 and pH 9.0
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SwissProt
brenda
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possibly loosely membrane-bound
brenda
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physiological function
TsrM can catalyze multiple turnovers in the absence of any reducing agent, but only when it is pre-loaded with methylcobalamin. When hydroxocobalamin or cob(II)alamin is bound to TsrM, a reductant is required to convert it to cob(I)alamin, which can acquire a methyl group directly from S-adenosylmethionine. TrsM is most active when flavodoxin/flavodoxin reductase/NADPH is included in the reaction
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TSRM_STRLU
599
0
66061
Swiss-Prot
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68554
x * 68554, SDS-PAGE
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4°C, 1 d, loss of 80% activity
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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Frenzel, T.; Zhou, P.; Floss, H.G.
Formation of 2-methyltryptophan in the biosynthesis of thiostrepton: isolation of S-adenosyl-methionine:tryptophan 2-methyltransferase
Arch. Biochem. Biophys.
278
35-40
1990
Streptomyces laurentii
brenda
Pierre, S.; Guillot, A.; Benjdia, A.; Sandstrm, C.; Langella, P.; Berteau, O.
Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes
Nat. Chem. Biol.
8
957-959
2012
Streptomyces laurentii (C0JRZ9)
brenda
Blaszczyk, A.; Knox, H.; Booker, S.
Understanding the role of electron donors in the reaction catalyzed by Tsrm, a cobalamin-dependent radical S-adenosylmethionine methylase
J. Biol. Inorg. Chem.
24
831-839
2019
Streptomyces laurentii (C0JRZ9)
brenda
Benjdia, A.; Pierre, S.; Gherasim, C.; Guillot, A.; Carmona, M.; Amara, P.; Banerjee, R.; Berteau, O.
The thiostrepton A tryptophan methyltransferase TsrM catalyses a cob(II)alamin-dependent methyl transfer reaction
Nat. Commun.
6
8377
2015
Streptomyces laurentii (C0JRZ9)
brenda