Information on EC 3.7.1.7 - beta-diketone hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.7.1.7
-
RECOMMENDED NAME
GeneOntology No.
beta-diketone hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
nonane-4,6-dione + H2O = pentan-2-one + butanoate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-C bond
SYSTEMATIC NAME
IUBMB Comments
nonane-4,6-dione acylhydrolase
Also acts on the product of the action of EC 1.1.3.18 secondary-alcohol oxidase, on polyvinyl alcohols; involved in the bacterial degradation of polyvinyl alcohol.
CAS REGISTRY NUMBER
COMMENTARY hide
97955-12-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
GenBank
Manually annotated by BRENDA team
isolated from PVA-rich soil, which was sampled at Pacific Textile Co., Jiangsu Province, China
-
-
Manually annotated by BRENDA team
strain 113P3
-
-
Manually annotated by BRENDA team
strain 113P3
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-phenyl-1,3-butanedione + H2O
acetic acid + acetophenone
show the reaction diagram
-
-
-
?
1-phenyl-2,4-butanedione + H2O
acetic acid + 1-phenyl-2-propanone
show the reaction diagram
-
-
-
?
2,4-hexanedione + H2O
acetic acid + 2-butanone
show the reaction diagram
2,4-nonanedione + H2O
acetic acid + 2-heptanone
show the reaction diagram
-
-
-
?
2,4-pentanedione + H2O
acetic acid + acetone
show the reaction diagram
3,5-heptanedione + H2O
propionic acid + 2-butanone
show the reaction diagram
3,5-nonanedione + H2O
propionic acid + 2-hexanone
show the reaction diagram
-
-
-
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
show the reaction diagram
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
5,7-dodecanedione + H2O
valeric acid + 2-hexanone
show the reaction diagram
-
-
-
?
6,8-tridecanedione + H2O
caproic acid + 2-heptanone
show the reaction diagram
-
-
-
?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
show the reaction diagram
bicyclo[2.2.2]octane-2,6-dione + H2O
[(S)-3-oxocyclohexyl]acetic acid
show the reaction diagram
desymmetrization of bicyclo[2.2.2]octane-2,6-dione
-
-
?
nonane-4,6-dione + H2O
pentan-2-one + butanoate
show the reaction diagram
-
-
-
?
oxidized polyvinyl alcohol + H2O
?
show the reaction diagram
p-nitrophenyl acetate + H2O
?
show the reaction diagram
polyvinyl alcohol + H2O
?
show the reaction diagram
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
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
nonane-4,6-dione + H2O
pentan-2-one + butanoate
show the reaction diagram
Q8YNV6
-
-
-
?
oxidized polyvinyl alcohol + H2O
?
show the reaction diagram
polyvinyl alcohol + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
-
slightly activates
Mg2+
-
slightly activates
Mn2+
-
stimulates the enzyme at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ba2+
-
slight inhibition at 1 mM
Ca2+
-
slight inhibition at 1 mM
Co2+
-
slight inhibition at 1 mM
Cr2+
-
moderate inhibition at 1 mM
Cu2+
-
slight inhibition at 1 mM
Fe2+
-
moderate inhibition at 1 mM
phenylmethanesulfonyl fluoride
-
strong inhibition
Sn2+
-
slight inhibition at 1 mM
Zn2+
-
appreciably inhibits
additional information
-
not inhibited by chelating agents, thiol agents and inhibitors of the respiratory chain
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000044
bicyclo[2.2.2]octane-2,6-dione
-
0.2
Oxidized polyvinyl alcohol
-
-
0.3
p-nitrophenyl acetate
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
bicyclo[2.2.2]octane-2,6-dione
Nostoc sp. PCC 7120
Q8YNV6
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
-
with oxidized polyvinyl alcohol as substrate
0.33
-
4,6-nonandione as substrate
1.65
-
oxidized polyvinyl alcohol as substrate
2.6
-
with p-nitrophenyl acetate as substrate
598
-
purified recombinant enzyme, substrate 4-nitrophenyl acetate, pH 8.0, 45°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
assay at
7.2 - 7.6
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
45
-
recombinant enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28800
predicted molecular mass
30000
determined by SDS-PAGE
40610
-
deduced from amino acid sequence
70000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the structure of beta-diketone hydrolase is determined to a resolution of 1.5 A in both native and ligand-bound forms
purified recombinant detagged wild-type enzyme and mutants S172A and S172C, free and in complexes with PEG, butyrate, or DMSO, respectively, by sitting drop method using 30% PEG 5000 MME, 0.1 M MES pH 6.5. and 0.2 M (NH4)2SO4 for the wild-type, and 0.1 M tri-sodium citrate, pH 5.6, 30% w/v PEG 4000, and 0.3% w/v n-octyl-beta-D-glucoside for the mutants, X-ray diffraction structure determination and analysis at 1.49-2.10 A resolution, molecular replacement
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
recombinant enzyme, stable at, over 90% activity remaning after 12 h, beyond this pH range, the OPH activity half-life is less than 1 h
733520
6.5 - 8.5
-
50 mM sodium phosphate or Tris/HCl buffer
675823
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
stable for 30 min, 50 mM Tris/HCl buffer, pH 8.0
45
-
recombinant enzyme, stable up to
47.5
-
recombinant enzyme, half-life is 5 h
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 1-67fold from Pichia pastoris strain GS115 culture supernatant by ultrafiltration, and hydrophobic interaction and cation exchange chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 trxB (DE3) by nickel affinity chromatography and digestion by TEV protease to remove the His-tagged thioredoxin, followed by a second nickel affinity chromatography, and anion exchange chromatography and ultrafiltration
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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to homogeneity, 5-9fold, gel filtration
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using a nickel affinity HiTRAP agarose column and a S200 16/60 Sephadex column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expression in Escherichia coli under the control of the lac promoter
-
expression of the OPH gene lacking the sequence encoding the original signal peptide in Escherichia coli strain BL21 (DE3), the recombinant enzyme is secreted, productivity of recombinant OPH reaches 565.95 U/L/h without and 733.17 U/L/h in presence of 200 mM glycine. Subcloning in Escherichia coli strain JM109. Therecombinant extracellular enzyme inhibits growth of Escherichia coli cells
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gene oph, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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gene oph, recombinant methano-inducible expression of the enzyme, ligated into the pPIC9K vector behind the alpha-factor signal sequence, in Pichia pastoris strain GS115
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into the pETYSBLIC vector for expression in Escherichia coli BL21DE3 cells
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 trxB (DE3)
-
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W255A
-
site-directed mutagenesis
W255F
-
site-directed mutagenesis
W255Y
-
site-directed mutagenesis
S172A
-
site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme
-
S172C
-
site-directed mutagenesis; site-directed mutagenesis, the mutant shows less than 10% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme
-
W255A
-
site-directed mutagenesis
-
W255Y
-
site-directed mutagenesis
-
C241A/C248A
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
molecular biology