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Information on EC 2.1.1.164 - demethylrebeccamycin-D-glucose O-methyltransferase for references in articles please use BRENDA:EC2.1.1.164
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IUBMB Comments Catalyses the last step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. The enzyme is able to use a wide variety substrates, tolerating variation on the imide heterocycle, deoxygenation of the sugar moiety, and even indolocarbazole glycoside anomers . The enzyme is a member of the general acid/base-dependent O-methyltransferase family .
The enzyme appears in viruses and cellular organisms
Synonyms
rebeccamycin MT, rebeccamycin O-methyltransferase,
RebM , RebM.,
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rebeccamycin O-methyltransferase
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RebM
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4'-demethylrebeccamycin + S-adenosyl-L-methionine = rebeccamycin + S-adenosyl-L-homocysteine
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-
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-
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S-adenosyl-L-methionine:demethylrebeccamycin-D-glucose O-methyltransferase
Catalyses the last step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. The enzyme is able to use a wide variety substrates, tolerating variation on the imide heterocycle, deoxygenation of the sugar moiety, and even indolocarbazole glycoside anomers [1]. The enzyme is a member of the general acid/base-dependent O-methyltransferase family [2].
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3-bromo-11-beta-D-glucopyranosyl-11,12-dihydroindolo[2,3-a]carbazole + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
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-
-
?
3-bromo-12-beta-D-glucopyranosyl-11,12-dihydroindolo[2,3-a]carbazole + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
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-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
dechlorinated 4'-demethyl-rebeccamycin + 5'-[[(3S)-3-amino-3-carboxypropyl](2-iodoethyl)ammonio]-5'-deoxyadenosine
dechlorinated rebeccamycin + ?
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-
-
-
?
dechlorinated 4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
dechlorinated rebeccamycin + S-adenosyl-L-homocysteine
dechlorinated 5-deoxo-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
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-
-
?
dechlorinated 6-methyl-2'-deoxy-4'-demethyl-alpha-D-Glc-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
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-
-
?
dechlorinated 6-methyl-2'-deoxy-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
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-
-
?
dechlorinated 6-[3-(1H-imidazol-1-yl)propyl]-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
-
-
-
?
dechlorinated 7-deoxo-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
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-
-
?
additional information
?
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RebM accepts a wide range of alternate substrates. Specifically, variation on the imide heterocycle by removal or addition of a bulky group is tolerated by RebM. Deoxygenation of the sugar moiety only slightly decreases RebM activity. RebM displays flexibility toward anomers and is able to process both alpha and beta-glycosidic analogues
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4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
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-
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
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-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
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-
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
last step in the biosynthesis of rebeccamycin
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?
dechlorinated 4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
dechlorinated rebeccamycin + S-adenosyl-L-homocysteine
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-
-
?
dechlorinated 4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
dechlorinated rebeccamycin + S-adenosyl-L-homocysteine
-
-
-
-
?
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4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
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-
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
last step in the biosynthesis of rebeccamycin
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?
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additional information
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RebM activity is not enhanced by divalent metals
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Ca2+
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1 mM, 8% inhibition
Co2+
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1 mM, 87% inhibition
Cu2+
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1 mM, 93% inhibition
EDTA
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1 mM, 5% inhibition
Fe2+
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1 mM, 17% inhibition
Mg2+
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1 mM, 3% inhibition
Mn2+
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1 mM, 48% inhibition
Ni2+
-
1 mM, complete inhibition
Zn2+
-
1 mM, complete inhibition
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0.0112 - 0.0798
4'-demethylrebeccamycin
0.0021
dechlorinated 4'-demethyl-rebeccamycin
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pH 8.0, 30°C
0.012 - 0.162
S-adenosyl-L-methionine
0.0112
4'-demethylrebeccamycin
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pH 8.0, 25°C, mutant enzyme H140A
0.016
4'-demethylrebeccamycin
-
pH 8.0, 25°C, mutant enzyme W134Y
0.017
4'-demethylrebeccamycin
-
pH 8.0, 25°C, mutant enzyme C70S
0.021
4'-demethylrebeccamycin
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pH 8.0, 25°C, mutant enzyme S138A
0.0215
4'-demethylrebeccamycin
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pH 8.0, 25°C, mutant enzyme L136V
0.0225
4'-demethylrebeccamycin
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pH 8.0, 25°C, mutant enzyme C70A
0.032
4'-demethylrebeccamycin
-
pH 8.0, 25°C, mutant enzyme D166A
0.0355
4'-demethylrebeccamycin
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pH 8.0, 25°C, wild-type enzyme
0.0535
4'-demethylrebeccamycin
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pH 8.0, 25°C, mutant enzyme P75S
0.0798
4'-demethylrebeccamycin
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pH 8.0, 25°C, mutant enzyme H141A
0.012
S-adenosyl-L-methionine
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pH 8.0, 30°C, cosubstrate: dechlorinated 4'-demethyl-rebeccamycin
0.012
S-adenosyl-L-methionine
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pH 8.0, 25°C, wild-type enzyme
0.017
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme C70A
0.018
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme S138A
0.0311
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme H140A
0.032
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme W134Y
0.0345
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme C70S
0.056
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme L136V
0.0943
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme H141A
0.162
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme D166A; pH 8.0, 25°C, mutant enzyme P75S
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0.047
dechlorinated 4'-demethyl-rebeccamycin
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pH 8.0, 30°C
0.0023 - 0.072
S-adenosyl-L-methionine
0.0023
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme H140A
0.005
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme D166A
0.0063
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme P75S
0.01
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme H141A
0.017
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme W134Y
0.023
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme S138A
0.025
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme L136V
0.047
S-adenosyl-L-methionine
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pH 8.0, 30°C, cosubstrate: dechlorinated 4'-demethyl-rebeccamycin
0.047
S-adenosyl-L-methionine
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pH 8.0, 25°C, wild-type enzyme
0.048
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme C70A
0.072
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme C70S
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0.031 - 3.9
S-adenosyl-L-methionine
0.031
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme D166A; pH 8.0, 25°C, mutant enzyme H140A/H141A
0.039
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme P75S
0.074
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme H140A
0.11
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme H141A
0.45
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme L136V
0.53
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme W134Y
1.28
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme S138A
2.09
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme C70S
2.8
S-adenosyl-L-methionine
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pH 8.0, 25°C, mutant enzyme C70A
3.9
S-adenosyl-L-methionine
-
pH 8.0, 25°C, wild-type enzyme
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6.5 - 8
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functional over a broader pH range from pH 6.5 to above 8.0
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UniProt
brenda
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-
-
brenda
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metabolism
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the enzyme is involved in rebeccamycin biosynthesis
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31400
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1 * 31400, calculated from sequence
32000
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1 * 32000, SDS-PAGE
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monomer
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1 * 31400, calculated from sequence; 1 * 32000, SDS-PAGE
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hanging drop vapor diffusion method at 20°C. The 2.65 A crystal structure of the rebeccamycin 4'-O-methyltransferase RebM in complex with S-adenosyl-L-homocysteine reveals RebM to adopt a typical S-adenosyl methionine binding fold of small molecule O-methyltransferases and display a weak dimerization domain unique to methyltransferases
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C70A
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kcat for S-adenosyl-L-methionine is nearly identical to wild-type value
C70S
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kcat for S-adenosyl-L-methionine is 1.53fold higher than wild-type value
D166A
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kcat for S-adenosyl-L-methionine is 10% of wild-type value
H140A
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kcat for S-adenosyl-L-methionine is 5% of wild-type value
H141A
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kcat for S-adenosyl-L-methionine is 21% of wild-type value
H149A/H141A
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activity is below the detection limit
L136V
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kcat for S-adenosyl-L-methionine is 54% of wild-type value
P75S
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although properly folded based upon CD spectroscopy, the mutant displays a substantially reduced affinity for AdoMet (about 10fold increase in Km). kcat for S-adenosyl-L-methionine is 13% of wild-type value
S138A
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kcat for S-adenosyl-L-methionine is 49% of wild-type value
W134Y
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kcat for S-adenosyl-L-methionine is 35% of wild-type value
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RebM expression is induced by the addition of isopropyl-beta-D-thiogalactopyranoside (0.4 mm final concentration)
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Zhang, C.; Albermann, C.; Fu, X.; Peters, N.R.; Chisholm, J.D.; Zhang, G.; Gilbert, E.J.; Wang, P.G.; van Vranken, D.L.; Thorson, J.S.
RebG- and RebM-catalyzed indolocarbazole diversification
Chembiochem
7
795-804
2006
Lentzea aerocolonigenes (Q8KZ94)
brenda
Zhang, C.; Weller, R.L.; Thorson, J.S.; Rajski, S.R.
Natural product diversification using a non-natural cofactor analogue of S-adenosyl-L-methionine
J. Am. Chem. Soc.
128
2760-2761
2006
Lentzea aerocolonigenes (Q8KZ94)
brenda
Singh, S.; McCoy, J.G.; Zhang, C.; Bingman, C.A.; Phillips, G.N. Jr.; Thorson, J.S.
Structure and mechanism of the rebeccamycin sugar 4'-O-methyltransferase RebM
J. Biol. Chem.
283
22628-22636
2008
Lentzea aerocolonigenes (Q8KZ94)
brenda
Singh, S.; Zhang, J.; Huber, T.D.; Sunkara, M.; Hurley, K.; Goff, R.D.; Wang, G.; Zhang, W.; Liu, C.; Rohr, J.; Van Lanen, S.G.; Morris, A.J.; Thorson, J.S.
Facile chemoenzymatic strategies for the synthesis and utilization of S-adenosyl-(L)-methionine analogues
Angew. Chem. Int. Ed. Engl.
53
3965-3969
2014
Lentzea aerocolonigenes
brenda
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Enzyme Nomenclature
2.1.1.164 demethylrebeccamycin-D-glucose O-methyltransferase
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