Information on EC 2.1.3.12 - decarbamoylnovobiocin carbamoyltransferase

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The expected taxonomic range for this enzyme is: Streptomyces niveus

EC NUMBER
COMMENTARY hide
2.1.3.12
-
RECOMMENDED NAME
GeneOntology No.
decarbamoylnovobiocin carbamoyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + decarbamoylnovobiocin = phosphate + novobiocin
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
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].
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 antibiotics, novobiocin
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
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the tandem action of CouL, CouM, CouP, and NovN generates a biscarbamoyl analogue of the pseudodimer coumermycin A1
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-
?
carbamoyl phosphate + decarbamoylnovobiocin
phosphate + novobiocin
show the reaction diagram
carbamoyl phosphate + novclobiocin 104
phosphate + ?
show the reaction diagram
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87% of novclobiocin 104 is converted to the carbamoylated derivative after overnight incubation
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?
carbamoyl phosphate + novclobiocin 105
phosphate + novclobiocin 115
show the reaction diagram
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?
carbamoyl phosphate + novclobiocin 107
phosphate + novclobiocin 117
show the reaction diagram
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?
carbamoyl phosphate + novclobiocin 108
phosphate + novclobiocin 118
show the reaction diagram
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-
-
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?
carbamoyl phosphate + novclobiocin 283
phosphate + novclobiocin 284
show the reaction diagram
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-
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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
carbamoyl phosphate + decarbamoylnovobiocin
phosphate + novobiocin
show the reaction diagram
-
the enzyme is involved in the biosynthesis of the aminocoumarin antibiotics, novobiocin
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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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+
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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
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pH 8.5, 22C
0.0024 - 0.0046
decarbamoylnovobiocin
0.0019
novclobiocin 104
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pH 8.0, 30C
0.0143
novclobiocin 105
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pH 8.0, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4 - 4.1
decarbamoylnovobiocin
1.32
novclobiocin 104
Streptomyces niveus
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pH 8.0, 30C
1.53
novclobiocin 105
Streptomyces niveus
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pH 8.0, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
891 - 1000
decarbamoylnovobiocin
10415
695
novclobiocin 104
Streptomyces niveus
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pH 8.0, 30C
42418
107
novclobiocin 105
Streptomyces niveus
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pH 8.0, 30C
42419
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
30
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
79000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 74499, calculated from sequence
monomer
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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
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N-terminal His6 fusion protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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overexpression in Streptomyces lividans as an N-terminal His6 fusion protein
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