Information on EC 2.1.1.315 - 27-O-demethylrifamycin SV methyltransferase

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The expected taxonomic range for this enzyme is: Amycolatopsis mediterranei

EC NUMBER
COMMENTARY hide
2.1.1.315
-
RECOMMENDED NAME
GeneOntology No.
27-O-demethylrifamycin SV methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 27-O-demethylrifamycin SV = S-adenosyl-L-homocysteine + rifamycin SV
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
rifamycin B biosynthesis
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Biosynthesis of ansamycins
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:27-O-demethylrifamycin-SV 27-O-methyltransferase
The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the antitubercular drug rifamycin B.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 27-O-demethylrifamycin SV
S-adenosyl-L-homocysteine + rifamycin SV
show the reaction diagram
additional information
?
-
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
S-adenosyl-L-methionine + 27-O-demethylrifamycin SV
S-adenosyl-L-homocysteine + rifamycin SV
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the purified enzyme does not require a divalent cation for catalytic activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
inhibits slightly
Co2+
-
strong inhibition
Mg2+
-
inhibits slightly
Ni2+
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strong inhibition
Zn2+
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strong inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
27-O-demethylrifamycin SV
-
pH 8.0, 30C
0.0193
S-adenosyl-L-methionine
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pH 8.0, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
87
27-O-demethylrifamycin SV
Amycolatopsis mediterranei
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pH 8.0, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4833
27-O-demethylrifamycin SV
Amycolatopsis mediterranei
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pH 8.0, 30C
197628
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
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pH 6.0: about 20% of maximal activity, pH 8.5: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
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non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a polyhistidine-tagged polypeptide
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