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Information on EC 2.1.1.285 - demethyldecarbamoylnovobiocin O-methyltransferase and Organism(s) Streptomyces niveus and UniProt Accession Q9L9F2

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IUBMB Comments
The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin.
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This record set is specific for:
Streptomyces niveus
UNIPROT: Q9L9F2
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The taxonomic range for the selected organisms is: Streptomyces niveus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
NovP, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:demethyldecarbamoylnovobiocin 4''-O-methyltransferase
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 SUBSTRATE
NATURAL 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
-
the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0095
demethyldecarbamoylnovobiocin
-
pH 8.5, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
demethyldecarbamoylnovobiocin
-
pH 8.5, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
42.1
demethyldecarbamoylnovobiocin
-
pH 8.5, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NOVP_STRNV
262
0
29967
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29967
x * 29967, calculated from sequence
32800
x * 32800, SDS-PAGE
66000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of recombinant NovP are grown by vapour diffusion
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminally His-tagged enzyme
His6-tagged protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stevenson, C.E.; Freel Meyers, C.L.; Walsh, C.T.; Lawson, D.M.
Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides
Acta Crystallogr. Sect. F
63
236-238
2007
Streptomyces niveus (Q9L9F2)
Manually annotated by BRENDA team
Freel Meyers, C.L.; Oberthr, M.; Xu, H.; Heide, L.; Kahne, D.; Walsh, C.T.
Characterization of NovP and NovN: completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring
Angew. Chem. Int. Ed. Engl.
43
67-70
2004
Streptomyces niveus
Manually annotated by BRENDA team
Gomez Garcia, I.; Stevenson, C.E.; Uson, I.; Freel Meyers, C.L.; Walsh, C.T.; Lawson, D.M.
The crystal structure of the novobiocin biosynthetic enzyme NovP: the first representative structure for the TylF O-methyltransferase superfamily
J. Mol. Biol.
395
390-407
2010
Streptomyces niveus (Q9L9F2)
Manually annotated by BRENDA team