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Information on EC 2.1.1.164 - demethylrebeccamycin-D-glucose O-methyltransferase and Organism(s) Lentzea aerocolonigenes and UniProt Accession Q8KZ94

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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 .
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This record set is specific for:
Lentzea aerocolonigenes
UNIPROT: Q8KZ94
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The taxonomic range for the selected organisms is: Lentzea aerocolonigenes
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
rebeccamycin MT, rebeccamycin O-methyltransferase, RebM, RebM., more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
rebeccamycin MT
-
-
rebeccamycin O-methyltransferase
-
-
RebM
-
-
-
-
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
?
3-bromo-12-beta-D-glucopyranosyl-11,12-dihydroindolo[2,3-a]carbazole + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
show the reaction diagram
dechlorinated 4'-demethyl-rebeccamycin + 5'-[[(3S)-3-amino-3-carboxypropyl](2-iodoethyl)ammonio]-5'-deoxyadenosine
dechlorinated rebeccamycin + ?
show the reaction diagram
-
-
-
?
dechlorinated 4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
dechlorinated rebeccamycin + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
dechlorinated 5-deoxo-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
dechlorinated 6-methyl-2'-deoxy-4'-demethyl-alpha-D-Glc-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
dechlorinated 6-methyl-2'-deoxy-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
dechlorinated 6-[3-(1H-imidazol-1-yl)propyl]-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
dechlorinated 7-deoxo-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
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
-
-
?
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
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
show the reaction diagram
4'-demethylrebeccamycin + S-adenosyl-L-methionine
rebeccamycin + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
RebM activity is not enhanced by divalent metals
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
1 mM, 8% inhibition
Co2+
1 mM, 87% inhibition
Cu2+
1 mM, 93% inhibition
EDTA
1 mM, 5% inhibition
Fe2+
1 mM, 17% inhibition
Mg2+
1 mM, 3% inhibition
Mn2+
1 mM, 48% inhibition
Ni2+
1 mM, complete inhibition
Zn2+
1 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0112 - 0.0798
4'-demethylrebeccamycin
0.0021
dechlorinated 4'-demethyl-rebeccamycin
pH 8.0, 30°C
0.012 - 0.162
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047
dechlorinated 4'-demethyl-rebeccamycin
pH 8.0, 30°C
0.0023 - 0.072
S-adenosyl-L-methionine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.031 - 3.9
S-adenosyl-L-methionine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
functional over a broader pH range from pH 6.5 to above 8.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme is involved in rebeccamycin biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
REBMT_LENAE
283
0
30374
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31400
1 * 31400, calculated from sequence
32000
1 * 32000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
H149A/H141A
activity is below the detection limit
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RebM expression is induced by the addition of isopropyl-beta-D-thiogalactopyranoside (0.4 mm final concentration)
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team