BRENDA home
History
Enzyme Nomenclature
Information on EC 2.1.1.164 - demethylrebeccamycin-D-glucose O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.164Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.1.1.164 demethylrebeccamycin-D-glucose O-methyltransferaseIUBMB 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 .
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RebM
RebM
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4'-demethylrebeccamycin + S-adenosyl-L-methionine = rebeccamycin + S-adenosyl-L-homocysteine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-bromo-11-beta-D-glucopyranosyl-11,12-dihydroindolo[2,3-a]carbazole + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
-
-
-
?
3-bromo-12-beta-D-glucopyranosyl-11,12-dihydroindolo[2,3-a]carbazole + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
-
-
-
?
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 + ?
-
-
-
?
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
-
-
-
?
dechlorinated 6-methyl-2'-deoxy-4'-demethyl-alpha-D-Glc-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
-
-
-
?
dechlorinated 6-methyl-2'-deoxy-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
-
-
-
?
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
-
-
-
?
additional information
?
-
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
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
-
-
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
-
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
last step in the biosynthesis of rebeccamycin
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
-
-
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
-
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
last step in the biosynthesis of rebeccamycin
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
RebM activity is not enhanced by divalent metals
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0112
4'-demethylrebeccamycin
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
pH 8.0, 25°C, mutant enzyme S138A
0.0215
4'-demethylrebeccamycin
pH 8.0, 25°C, mutant enzyme L136V
0.0225
4'-demethylrebeccamycin
pH 8.0, 25°C, mutant enzyme C70A
0.032
4'-demethylrebeccamycin
pH 8.0, 25°C, mutant enzyme D166A
0.0355
4'-demethylrebeccamycin
pH 8.0, 25°C, wild-type enzyme
0.0535
4'-demethylrebeccamycin
pH 8.0, 25°C, mutant enzyme P75S
0.0798
4'-demethylrebeccamycin
pH 8.0, 25°C, mutant enzyme H141A
0.012
S-adenosyl-L-methionine
pH 8.0, 30°C, cosubstrate: dechlorinated 4'-demethyl-rebeccamycin
0.017
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme C70A
0.018
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme S138A
0.0311
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme H140A
0.032
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme W134Y
0.0345
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme C70S
0.056
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme L136V
0.0943
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme H141A
0.162
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme D166A
0.162
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme P75S
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme H140A
0.005
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme D166A
0.0063
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme P75S
0.01
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme H141A
0.017
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme W134Y
0.023
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme S138A
0.025
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme L136V
0.047
S-adenosyl-L-methionine
pH 8.0, 30°C, cosubstrate: dechlorinated 4'-demethyl-rebeccamycin
0.048
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme C70A
0.072
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme C70S
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.031
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme D166A
0.031
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme H140A/H141A
0.039
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme P75S
0.074
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme H140A
0.11
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme H141A
0.45
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme L136V
0.53
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme W134Y
1.28
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme S138A
2.09
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme C70S
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
functional over a broader pH range from pH 6.5 to above 8.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Show AA Sequence and Transmembrane Helices (1191 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C70A
kcat for S-adenosyl-L-methionine is nearly identical to wild-type value
C70S
kcat for S-adenosyl-L-methionine is 1.53fold higher than wild-type value
D166A
kcat for S-adenosyl-L-methionine is 10% of wild-type value
H140A
kcat for S-adenosyl-L-methionine is 5% of wild-type value
H141A
kcat for S-adenosyl-L-methionine is 21% of wild-type value
L136V
kcat for S-adenosyl-L-methionine is 54% of wild-type value
P75S
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
kcat for S-adenosyl-L-methionine is 49% of wild-type value
W134Y
kcat for S-adenosyl-L-methionine is 35% of wild-type value
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RebM expression is induced by the addition of isopropyl-beta-D-thiogalactopyranoside (0.4 mm final concentration)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.1.1.164)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda4 Ver: 9edf756-main (2022-05-17 10:30:03 +0200)