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Information on EC 2.1.3.12 - decarbamoylnovobiocin carbamoyltransferase and Organism(s) Streptomyces niveus and UniProt Accession Q9L9F4

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IUBMB Comments
The enzyme catalyses the last step in the biosynthesis of the aminocoumarin antibiotic novobiocin. The reaction is activated by ATP .
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This record set is specific for:
Streptomyces niveus
UNIPROT: Q9L9F4
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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
NovN, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
carbamoyl phosphate:decarbamoylnovobiocin 3''-O-carbamoyltransferase
The enzyme catalyses the last step in the biosynthesis of the aminocoumarin antibiotic novobiocin. The reaction is activated by ATP [1].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 carbamoyl phosphate + N,N'-bis(7-[[(2R,3R,4S,5R)-3,4-dihydroxy-5-methoxy-6,6-dimethyltetrahydro-2H-pyran-2-yl]oxy]-4-hydroxy-8-methyl-2-oxo-2H-chromen-3-yl)-3-methyl-1H-pyrrole-2,4-dicarboxamide
2 phosphate + (3-methyl-1H-pyrrole-2,4-diyl)bis[carbonylimino(4-hydroxy-8-methyl-2-oxo-2H-chromene-3,7-diyl)oxy-(2R,3R,4S,5R)-3-hydroxy-5-methoxy-6,6-dimethyltetrahydro-2H-pyran-2,4-diyl] dicarbamate
show the reaction diagram
-
the tandem action of CouL, CouM, CouP, and NovN generates a biscarbamoyl analogue of the pseudodimer coumermycin A1
-
-
?
carbamoyl phosphate + decarbamoylnovobiocin
phosphate + novobiocin
show the reaction diagram
carbamoyl phosphate + novclobiocin 104
phosphate + ?
show the reaction diagram
-
87% of novclobiocin 104 is converted to the carbamoylated derivative after overnight incubation
-
-
?
carbamoyl phosphate + novclobiocin 105
phosphate + novclobiocin 115
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + novclobiocin 107
phosphate + novclobiocin 117
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + novclobiocin 108
phosphate + novclobiocin 118
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + novclobiocin 283
phosphate + novclobiocin 284
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
carbamoyl phosphate + decarbamoylnovobiocin
phosphate + novobiocin
show the reaction diagram
-
the enzyme is involved in the biosynthesis of the aminocoumarin antibiotics, novobiocin
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
the enzyme is strictly dependent on the presence ATP and divalent cations such as Mg2+ or Mn2+. Optimal concentrations of both Mg2+ and ATP is 2 mM
Mn2+
-
the enzyme is strictly dependent on the presence ATP and divalent cations such as Mg2+ or Mn2+. Optimal concentrations of both Mg2+ and ATP is 2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0051
Carbamoyl phosphate
-
pH 8.5, 22°C
0.0024 - 0.0046
decarbamoylnovobiocin
0.0019
novclobiocin 104
-
pH 8.0, 30°C
0.0143
novclobiocin 105
-
pH 8.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4 - 4.1
decarbamoylnovobiocin
1.32
novclobiocin 104
-
pH 8.0, 30°C
1.53
novclobiocin 105
-
pH 8.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
891 - 1000
decarbamoylnovobiocin
695
novclobiocin 104
-
pH 8.0, 30°C
107
novclobiocin 105
-
pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme is involved in the biosynthesis of the aminocoumarin antibiotics, novobiocin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NOVN_STRNV
677
0
74340
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74499
x * 74499, calculated from sequence
78500
-
1 * 78500, calculated from sequence
79000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 74499, calculated from sequence
monomer
-
1 * 78500, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapour diffusion method. Crystallized in two different crystal forms. Crystal form I belongs to space group C2 and native data are collected to 2.9 A resolution. Crystal form II has I-centred orthorhombic symmetry and native data are recorded to a resolution of 2.3 A at a synchrotron
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-His6-tagged protein
-
N-terminal His6 fusion protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
overexpression in Streptomyces lividans as an N-terminal His6 fusion protein
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gomez Garcia, I.; Freel Meyers, C.L.; Walsh, C.T.; Lawson, D.M.
Crystallization and preliminary X-ray analysis of the O-carbamoyltransferase NovN from the novobiocin-biosynthetic cluster of Streptomyces spheroides
Acta Crystallogr. Sect. F
64
1000-1002
2008
Streptomyces niveus (Q9L9F4)
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
Freel Meyers, C.L.; Oberthr, M.; Heide, L.; Kahne, D.; Walsh, C.T.
Assembly of dimeric variants of coumermycins by tandem action of the four biosynthetic enzymes CouL, CouM, CouP, and NovN
Biochemistry
43
15022-15036
2004
Streptomyces niveus
Manually annotated by BRENDA team
Xu, H.; Heide, L.; Li, S.M.
New aminocoumarin antibiotics formed by a combined mutational and chemoenzymatic approach utilizing the carbamoyltransferase NovN
Chem. Biol.
11
655-662
2004
Streptomyces niveus
Manually annotated by BRENDA team