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Information on EC 3.7.1.7 - beta-diketone hydrolase
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3.7.1.7 beta-diketone hydrolaseIUBMB Comments
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.
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Word Map
- 3.7.1.7
- sphingopyxis
-
textile
- putida
- lipase
-
sludge
-
shake
-
cytochemically
-
ache
-
desizing
- acetylacetone
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gly-x-ser-x-gly
- p-nitrophenyl
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alpha-granules
- caprylate
- industry
-
wastewater
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hydrolysed
- pmsf
- sphingomonas
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depolymerases
- dt
- molecular biology
The enzyme appears in viruses and cellular organisms
Synonyms
pva-degrading enzyme, pvaase, oxidized pva hydrolase, oxidized polyvinyl alcohol hydrolase, poly(vinyl alcohol) (pva)-degrading enzyme, beta-diketone hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
OPH
OPH hydrolase
oxidized polyvinyl alcohol hydrolase
oxidized PVA hydrolase
poly(vinyl alcohol) (PVA)-degrading enzyme
pOPH
PVA-degrading enzyme
PVAase
oxidized polyvinyl alcohol hydrolase
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oxidized PVA hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nonane-4,6-dione + H2O = pentan-2-one + butanoate
putative serine hydrolase
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nonane-4,6-dione + H2O = pentan-2-one + butanoate
reaction mechanism, the reaction catalyzed by OPH is typical of alpha/beta-hydrolases, except that the cleaved bond is between two carbon atoms. Here electron delocalization seems to play an essential role. Upon C-C bond breaking, the negative charge on CO1' is probably stabilized by hydrogen bonds to the backbone NH of Ser66 and Val67, thus forming a second oxyanion hole. This anion-binding beta3-alpha1 loop might promote spontaneous oxidation of Cys172 to a sulfonate
nonane-4,6-dione + H2O = pentan-2-one + butanoate
reaction mechanism, the reaction catalyzed by OPH is typical of alpha/beta-hydrolases, except that the cleaved bond is between two carbon atoms. Here electron delocalization seems to play an essential role. Upon C-C bond breaking, the negative charge on CO1' is probably stabilized by hydrogen bonds to the backbone NH of Ser66 and Val67, thus forming a second oxyanion hole. This anion-binding beta3-alpha1 loop might promote spontaneous oxidation of Cys172 to a sulfonate
nonane-4,6-dione + H2O = pentan-2-one + butanoate
putative serine hydrolase
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nonane-4,6-dione + H2O = pentan-2-one + butanoate
reaction mechanism, the reaction catalyzed by OPH is typical of alpha/beta-hydrolases, except that the cleaved bond is between two carbon atoms. Here electron delocalization seems to play an essential role. Upon C-C bond breaking, the negative charge on CO1' is probably stabilized by hydrogen bonds to the backbone NH of Ser66 and Val67, thus forming a second oxyanion hole. This anion-binding beta3-alpha1 loop might promote spontaneous oxidation of Cys172 to a sulfonate
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nonane-4,6-dione + H2O = pentan-2-one + butanoate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-C bond
hydrolysis of C-C bond
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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.
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CAS REGISTRY NUMBER
COMMENTARY
97955-12-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-phenyl-2,4-butanedione + H2O
acetic acid + 1-phenyl-2-propanone
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?
bicyclo[2.2.2]octane-2,6-dione + H2O
[(S)-3-oxocyclohexyl]acetic acid
desymmetrization of bicyclo[2.2.2]octane-2,6-dione
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-
?
nonane-4,6-dione + H2O
pentan-2-one + butanoate
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?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
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?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
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?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
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?
additional information
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the enzyme catalyzes the cleavage of C-C bond in beta-diketone
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?
additional information
?
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the enzyme catalyzes the cleavage of C-C bond in beta-diketone
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?
additional information
?
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the enzyme shows lipase activity with 4-nitrophenyl esters as the substrates. The wild-type enzyme shows increased Km and decreased kcat/Km with the acyl chain length, and the mutants show reduced kcat/Km for 4-nitrophenyl acetate, indicating the importance of Trp255 in sequestering the active site from solvent. The significantly lower activity for 4-nitrophenyl butyrate can be a result of product inhibition
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?
additional information
?
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the enzyme shows lipase activity with 4-nitrophenyl esters as the substrates. The wild-type enzyme shows increased Km and decreased kcat/Km with the acyl chain length, and the mutants show reduced kcat/Km for 4-nitrophenyl acetate, indicating the importance of Trp255 in sequestering the active site from solvent. The significantly lower activity for 4-nitrophenyl butyrate can be a result of product inhibition
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?
additional information
?
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the formation of hydrogen bonds between Gly65, Ser66, Val67 with ligand exert extremely important promotion effect on the reaction. Besides, significant electrostatic influence of Glu198 also contributes to the catalysis
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additional information
?
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no activity towards pentane-2,4-dione
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?
additional information
?
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the enzyme catalyzes the cleavage of C-C bond in beta-diketone
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?
additional information
?
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the enzyme shows lipase activity with 4-nitrophenyl esters as the substrates. The wild-type enzyme shows increased Km and decreased kcat/Km with the acyl chain length, and the mutants show reduced kcat/Km for 4-nitrophenyl acetate, indicating the importance of Trp255 in sequestering the active site from solvent. The significantly lower activity for 4-nitrophenyl butyrate can be a result of product inhibition
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?
additional information
?
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no activity on monoketones, diketones and esters
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?
additional information
?
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no activity on monoketones, diketones and esters
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?
additional information
?
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the enzyme catalyzes the cleavage of C-C bond in beta-diketone
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?
additional information
?
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the enzyme shows lipase activity with 4-nitrophenyl esters as the substrates. The wild-type enzyme shows increased Km and decreased kcat/Km with the acyl chain length
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nonane-4,6-dione + H2O
pentan-2-one + butanoate
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?
additional information
?
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the enzyme catalyzes the cleavage of C-C bond in beta-diketone
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?
additional information
?
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the enzyme catalyzes the cleavage of C-C bond in beta-diketone
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?
additional information
?
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the enzyme catalyzes the cleavage of C-C bond in beta-diketone
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?
additional information
?
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the enzyme catalyzes the cleavage of C-C bond in beta-diketone
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by chelating agents, thiol agents and inhibitors of the respiratory chain
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics of the recombinant enzyme with 4-nitrophenyl acetate as substrate
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additional information
additional information
Michaelis-Menten kinetics of the wild-type enzyme with 4-nitrophenyl fatty acid (C2-C16) substrates, overview
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additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes with 4-nitrophenyl fatty acid (C2-C16) substrates, overview
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additional information
additional information
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Michaelis-Menten kinetics of wild-type and mutant enzymes with 4-nitrophenyl fatty acid (C2-C16) substrates, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
598
purified recombinant enzyme, substrate 4-nitrophenyl acetate, pH 8.0, 45°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from PVA-rich soil, which was sampled at Pacific Textile Co., Jiangsu Province, China
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brenda
isolated from PVA-rich soil, which was sampled at Pacific Textile Co., Jiangsu Province, China
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brenda
isolated from PVA-rich soil, which was sampled at Pacific Textile Co., Jiangsu Province, China
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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batch cultivation of a mixed culture at different pH values, Pseudomonas sp. OPH is most active, 2.11 U/ml, and stable at pH values between pH 6.0 and pH 7.0, highest production rate at pH 7.0 with 44.2 U/g/h, two-stage pH control strategy, overview
brenda
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batch cultivation of a mixed culture at different pH values, Pseudomonas sp. OPH is most active, 2.11 U/ml, and stable at pH values between pH 6.0 and pH 7.0, two-stage pH control strategy, overview
brenda
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batch cultivation of a mixed culture at different pH values, Pseudomonas sp. OPH is most active, 2.11 U/ml, and stable at pH values between pH 6.0 and pH 7.0, highest production rate at pH 7.0 with 44.2 U/g/h, two-stage pH control strategy, overview
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brenda
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batch cultivation of a mixed culture at different pH values, Pseudomonas sp. OPH is most active, 2.11 U/ml, and stable at pH values between pH 6.0 and pH 7.0, two-stage pH control strategy, overview
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brenda
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batch cultivation of a mixed culture at different pH values, Pseudomonas sp. OPH is most active, 2.11 U/ml, and stable at pH values between pH 6.0 and pH 7.0, highest production rate at pH 7.0 with 44.2 U/g/h, two-stage pH control strategy, overview
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brenda
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batch cultivation of a mixed culture at different pH values, Pseudomonas sp. OPH is most active, 2.11 U/ml, and stable at pH values between pH 6.0 and pH 7.0, two-stage pH control strategy, overview
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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specific activity in membrane fraction is several times higher than that of soluble fraction
brenda
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specific activity in membrane fraction is several times higher than that of soluble fraction
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
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oxidized polyvinyl alcohol hydrolase is a key enzyme in the degradation of polyvinyl alcohol
physiological function
additional information
evolution
the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site
evolution
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the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site
evolution
the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site
evolution
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the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site
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physiological function
the enzyme is involved in degradation of polyvinyl alcohol
physiological function
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the enzyme is involved in degradation of polyvinyl alcohol
physiological function
the enzyme is involved in degradation of polyvinyl alcohol
physiological function
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the enzyme is involved in degradation of polyvinyl alcohol
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additional information
roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase, the lid is the most variable region of the enzyme. The disulfide bond formation of Cys257/267 is important for the activity of pOPH
additional information
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roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase, the lid is the most variable region of the enzyme. The disulfide bond formation of Cys257/267 is important for the activity of pOPH
additional information
roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase, the lid is the most variable region of the enzyme. The disulfide bond formation of Cys257/267 is not essential for sOPH, which has a shorter lid structure
additional information
substrate binding and catalysis, enzyme modeling, overview
additional information
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substrate binding and catalysis, enzyme modeling, overview
additional information
substrate binding and catalysis, enzyme modeling, overview
additional information
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roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase, the lid is the most variable region of the enzyme. The disulfide bond formation of Cys257/267 is important for the activity of pOPH
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additional information
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substrate binding and catalysis, enzyme modeling, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A1V5BRX0_9DELT
339
0
37022
TrEMBL
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A0A2Z2NUM5_9GAMM
340
0
36512
TrEMBL
-
A0A1V4WJI2_9DELT
310
0
33944
TrEMBL
-
A0A518B2F2_9BACT
307
0
33509
TrEMBL
-