Information on EC 2.1.1.164 - demethylrebeccamycin-D-glucose O-methyltransferase

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The expected taxonomic range for this enzyme is: Lechevalieria aerocolonigenes

EC NUMBER
COMMENTARY hide
2.1.1.164
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RECOMMENDED NAME
GeneOntology No.
demethylrebeccamycin-D-glucose O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4'-demethylrebeccamycin + S-adenosyl-L-methionine = rebeccamycin + S-adenosyl-L-homocysteine
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
rebeccamycin biosynthesis
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Staurosporine biosynthesis
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Biosynthesis of antibiotics
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme is involved in rebeccamycin biosynthesis
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
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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
show the reaction diagram
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-
-
?
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
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-
-
-
?
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
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-
-
?
dechlorinated 6-methyl-2'-deoxy-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
show the reaction diagram
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-
-
?
dechlorinated 6-[3-(1H-imidazol-1-yl)propyl]-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
show the reaction diagram
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-
-
?
dechlorinated 7-deoxo-4'-demethyl-rebeccamycin + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
show the reaction diagram
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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RebM activity is not enhanced by divalent metals
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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+
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1 mM, complete inhibition
Zn2+
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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
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pH 8.0, 30C
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
Lechevalieria aerocolonigenes
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pH 8.0, 30C
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
24
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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functional over a broader pH range from pH 6.5 to above 8.0
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 31400, calculated from sequence; 1 * 32000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 20C. 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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RebM expression is induced by the addition of isopropyl-beta-D-thiogalactopyranoside (0.4 mm final concentration)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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