Information on EC 2.1.1.285 - demethyldecarbamoylnovobiocin O-methyltransferase

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The expected taxonomic range for this enzyme is: Streptomyces niveus

EC NUMBER
COMMENTARY hide
2.1.1.285
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RECOMMENDED NAME
GeneOntology No.
demethyldecarbamoylnovobiocin O-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + demethyldecarbamoylnovobiocin = S-adenosyl-L-homocysteine + decarbamoylnovobiocin
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
novobiocin biosynthesis
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Novobiocin biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:demethyldecarbamoylnovobiocin 4''-O-methyltransferase
The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin
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 + demethyldecarbamoylnovobiocin
S-adenosyl-L-homocysteine + decarbamoylnovobiocin
show the reaction diagram
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 + demethyldecarbamoylnovobiocin
S-adenosyl-L-homocysteine + decarbamoylnovobiocin
show the reaction diagram
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the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0095
demethyldecarbamoylnovobiocin
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pH 8.5, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
demethyldecarbamoylnovobiocin
Streptomyces niveus
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pH 8.5, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
42.1
demethyldecarbamoylnovobiocin
Streptomyces niveus
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pH 8.5, 22°C
28940
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 29967, calculated from sequence; x * 32800, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of recombinant NovP are grown by vapour diffusion
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high resolution crystal structure of NovP as a binary complex with its desmethylated co-substrate, S-adenosyl-L-homocysteine. The structure includes a helical lid region that gates access to the co-substrate binding pocket, and an active centre that contains a 3-Asp putative metal-binding site. A further conserved Asp likely acts as the general base that initiates the reaction by deprotonating the 4-OH group of the noviose unit. Models suggest that NovP is unlikely to tolerate significant modifications at the noviose moiety, but could show increasing substrate promiscuity as a function of the distance of the modification from the methylation site. These observations could inform future attempts to utilise NovP for methylating a range of glycosylated compounds
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-tagged protein
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N-terminally His-tagged enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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