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Information on EC 2.1.1.106 - tryptophan 2-C-methyltransferase and Organism(s) Streptomyces laurentii and UniProt Accession C0JRZ9

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.106 tryptophan 2-C-methyltransferase
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.
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Streptomyces laurentii
UNIPROT: C0JRZ9
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thiostrepton A tryptophan methyltransferase
-
thiostrepton tryptophan methyltransferase
-
S-adenosylmethionine:tryptophan 2-methyltransferase
-
-
-
-
tryptophan 2-methyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
126626-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 3-methylindole
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + D-tryptophan
S-adenosyl-L-homocysteine + D-2-methyltryptophan
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + L-5-fluoro-tryptophan
S-adenosyl-L-homocysteine + L-5-fluoro-2-methyltryptophan
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + L-5-hydroxy-tryptophan
S-adenosyl-L-homocysteine + L-5-hydroxy-2-methyltryptophan
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + L-5-methyl-tryptophan
S-adenosyl-L-homocysteine + L-2,5-dimethyltryptophan
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + L-tryptophan
S-adenosyl-L-homocysteine + L-2-methyltryptophan
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + melatonin
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + serotonin
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + D,L-tryptophan
S-adenosyl-L-homocysteine + D,L-2-methyltryptophan
show the reaction diagram
-
significant slower reaction rate with D-tryptophan
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + L-tryptophan
S-adenosyl-L-homocysteine + L-2-methyltryptophan
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-deoxyadenosylcobalamin
5'-deoxyadenosylcob(III)alamin may substitute for methylcob(III)alamin, albeit only in the presence of light
hydroxycobalamin
-
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
contains cobalt
Iron
contains iron
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Methyltryptophan
-
product inhibition
S-adenosyl-L-homocysteine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
S-adenosyl-L-methionine
-
cell free extract
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48
S-adenosyl-L-homocysteine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
cell free extract
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 9
-
half-maximal activity at pH 6.8 and pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
possibly loosely membrane-bound
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TSRM_STRLU
599
0
66061
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68554
x * 68554, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 68554, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
half-life: 2 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1 d, loss of 80% activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team