Any feedback?
No. of entries
Information on EC 2.1.1.164 - demethylrebeccamycin-D-glucose O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.164
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.164 demethylrebeccamycin-D-glucose O-methyltransferase
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 expected taxonomic range for this enzyme is: Lentzea aerocolonigenes
Reaction Schemes
showSynonyms
rebeccamycin MT, rebeccamycin O-methyltransferase, RebM, RebM., more
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
rebeccamycin biosynthesis
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
LITERATURE
COMMENTARY
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
Substrates: -
Products: -
Products: -
?
3-bromo-12-beta-D-glucopyranosyl-11,12-dihydroindolo[2,3-a]carbazole + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
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 + ?
Substrates: -
Products: -
Products: -
?
dechlorinated 4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
dechlorinated rebeccamycin + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
dechlorinated 5-deoxo-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
dechlorinated 6-methyl-2'-deoxy-4'-demethyl-alpha-D-Glc-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
dechlorinated 6-methyl-2'-deoxy-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
dechlorinated 6-[3-(1H-imidazol-1-yl)propyl]-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
dechlorinated 7-deoxo-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
Substrates: last step in the biosynthesis of rebeccamycin
Products: -
Products: -
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
-
Substrates: -
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
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
Substrates: last step in the biosynthesis of rebeccamycin
Products: -
Products: -
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
-
Substrates: -
Products: -
Products: -
?
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
0.0535
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 P75S
0.162
S-adenosyl-L-methionine
pH 8.0, 25°C, mutant enzyme D166A
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
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). REBMT_LENAE
283
0
30374
Swiss-Prot
other Location (Reliability: 2)
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
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.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
