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Information on EC 3.7.1.7 - beta-diketone hydrolase
for references in articles please use BRENDA:EC3.7.1.7
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EC Tree 3 Hydrolases
3.7 Acting on carbon-carbon bonds
3.7.1 In ketonic substances
3.7.1.7 beta-diketone hydrolase
IUBMB 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.
The enzyme appears in viruses and cellular organisms
- 3.7.1.7
- sphingopyxis
-
textile
- putida
- lipase
-
sludge
-
shake
-
cytochemically
-
ache
-
desizing
- acetylacetone
-
gly-x-ser-x-gly
- p-nitrophenyl
-
alpha-granules
- caprylate
- industry
-
wastewater
-
hydrolysed
- pmsf
- sphingomonas
-
depolymerases
- dt
- molecular biology
showSynonyms
pva-degrading enzyme, pvaase, oxidized pva hydrolase, oxidized polyvinyl alcohol hydrolase, beta-diketone hydrolase, poly(vinyl alcohol) (pva)-degrading enzyme, more
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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
-
-
-
-
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
-
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
-
-
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
-
-
-
-
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-phenyl-1,3-butanedione + H2O
acetic acid + acetophenone
-
Substrates: -
Products: -
Products: -
?
1-phenyl-2,4-butanedione + H2O
acetic acid + 1-phenyl-2-propanone
-
Substrates: -
Products: -
Products: -
?
2,4-nonanedione + H2O
acetic acid + 2-heptanone
-
Substrates: -
Products: -
Products: -
?
3,5-nonanedione + H2O
propionic acid + 2-hexanone
-
Substrates: -
Products: -
Products: -
?
5,7-dodecanedione + H2O
valeric acid + 2-hexanone
-
Substrates: -
Products: -
Products: -
?
6,8-tridecanedione + H2O
caproic acid + 2-heptanone
-
Substrates: -
Products: -
Products: -
?
bicyclo[2.2.2]octane-2,6-dione + H2O
[(S)-3-oxocyclohexyl]acetic acid
Q8YNV6
Substrates: desymmetrization of bicyclo[2.2.2]octane-2,6-dione
Products: -
Products: -
?
nonane-4,6-dione + H2O
pentan-2-one + butanoate
Q8YNV6
Substrates: -
Products: -
Products: -
?
2,4-hexanedione + H2O
acetic acid + 2-butanone
-
Substrates: -
Products: -
Products: -
?
2,4-hexanedione + H2O
acetic acid + 2-butanone
-
Substrates: -
Products: -
Products: -
?
2,4-pentanedione + H2O
acetic acid + acetone
-
Substrates: -
Products: -
Products: -
?
2,4-pentanedione + H2O
acetic acid + acetone
-
Substrates: -
Products: -
Products: -
?
3,5-heptanedione + H2O
propionic acid + 2-butanone
-
Substrates: -
Products: -
Products: -
?
3,5-heptanedione + H2O
propionic acid + 2-butanone
-
Substrates: -
Products: -
Products: -
?
3,5-heptanedione + H2O
propionic acid + 2-butanone
-
Substrates: -
Products: -
Products: -
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
-
Substrates: -
Products: -
Products: -
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
Sphingopyxis sp. M19
-
Substrates: -
Products: -
Products: -
?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
-
Substrates: -
Products: -
Products: -
?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
-
Substrates: -
Products: -
Products: -
?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
-
Substrates: -
Products: -
Products: -
?
oxidized polyvinyl alcohol + H2O
?
Substrates: -
Products: -
Products: -
?
oxidized polyvinyl alcohol + H2O
?
Substrates: -
Products: -
Products: -
?
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
-
Substrates: -
Products: -
Products: -
?
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
-
Substrates: -
Products: -
Products: -
?
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity towards pentane-2,4-dione
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the cleavage of C-C bond in beta-diketone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the cleavage of C-C bond in beta-diketone
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity towards pentane-2,4-dione
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the cleavage of C-C bond in beta-diketone
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity on monoketones, diketones and esters
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity on monoketones, diketones and esters
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the cleavage of C-C bond in beta-diketone
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nonane-4,6-dione + H2O
pentan-2-one + butanoate
Q8YNV6
Substrates: -
Products: -
Products: -
?
oxidized polyvinyl alcohol + H2O
?
Substrates: -
Products: -
Products: -
?
oxidized polyvinyl alcohol + H2O
?
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the cleavage of C-C bond in beta-diketone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the cleavage of C-C bond in beta-diketone
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the cleavage of C-C bond in beta-diketone
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the cleavage of C-C bond in beta-diketone
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ni2+
Sphingopyxis sp. M19
-
rapid decreases in relative enzyme activity at 2 mM. The enzyme activity is completely lost at 16 mM
additional information
-
not inhibited by chelating agents, thiol agents and inhibitors of the respiratory chain
-
Co2+
Sphingopyxis sp. M19
-
rapid decreases in relative enzyme activity at 2 mM. The enzyme activity is completely lost at 16 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes with 4-nitrophenyl fatty acid (C2-C16) substrates, overview
-
additional information
additional information
-
Michaelis-Menten kinetics of wild-type and mutant enzymes with 4-nitrophenyl fatty acid (C2-C16) substrates, overview
-
additional information
additional information
Michaelis-Menten kinetics of the wild-type enzyme with 4-nitrophenyl fatty acid (C2-C16) substrates, overview
-
additional information
additional information
Michaelis-Menten kinetics of the recombinant enzyme with 4-nitrophenyl acetate as substrate
-
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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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
-
-
brenda
isolated from PVA-rich soil, which was sampled at Pacific Textile Co., Jiangsu Province, China
-
-
brenda
isolated from PVA-rich soil, which was sampled at Pacific Textile Co., Jiangsu Province, China
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
-
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
-
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
-
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
-
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
-
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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
specific activity in membrane fraction is several times higher than that of soluble fraction
brenda
-
specific activity in membrane fraction is several times higher than that of soluble fraction
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
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
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
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
-
metabolism
-
oxidized polyvinyl alcohol hydrolase is a key enzyme in the degradation of polyvinyl alcohol
metabolism
Sphingopyxis sp. M19
-
the enzyme plays an important role in the pathway of polyvinyl alcohol biodegradation
physiological function
the enzyme is involved in degradation of polyvinyl alcohol
physiological function
the enzyme is involved in degradation of polyvinyl alcohol
physiological function
the enzyme is involved in degradation of polyvinyl alcohol
physiological function
the enzyme is involved in degradation of polyvinyl alcohol
physiological function
-
the enzyme is involved in degradation of polyvinyl alcohol
-
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
-
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
-
substrate binding and catalysis, enzyme modeling, overview
additional information
substrate binding and catalysis, enzyme modeling, overview
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
-
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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
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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
Q8YNV6
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S172A
S172C
S172A
S172C
C241A/C248A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
additional information
S172A
site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme
S172A
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, the mutant shows less than 10% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme
S172A
-
site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme
-
S172A
-
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, the mutant shows less than 10% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme
-
additional information
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. The mutant activity is retained with 4-nitrophenyl caprylate and 4-nitrophenyl laurate as the substrates, reflecting the amphipathic nature of the cleft
additional information
-
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. The mutant activity is retained with 4-nitrophenyl caprylate and 4-nitrophenyl laurate as the substrates, reflecting the amphipathic nature of the cleft
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
Sphingopyxis sp. M19
-
the lowest relative enzyme activity is 78.79% (reaction system pH 4.0) and the highest is 95.84% (reaction system pH 11.0) after 1 h of incubation. After 3 h, the relative enzyme activity decreases to 56.01% (pH 4.0), 61.88% (pH 6.0), 67.11% (pH 7.0), 76.5% (pH 9.0), and 84.58% (pH 11.0). When the reaction lasts for 8 h, only the relative enzyme activity in an environment with an alkaline pH exceeds 50%
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 70
Sphingopyxis sp. M19
-
at 25°C and 37°C, the enzyme activity does not decrease significantly and the relative enzyme activity remains more than 60% at 8 h. At 50°C, the relative enzyme activity in a 1 h reaction decreases to less than 60%, whereas at 60°C and 70°C, the relative enzyme activity is 50% after a 1 h reaction
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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
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
using a nickel affinity HiTRAP agarose column and a S200 16/60 Sephadex column
Q8YNV6
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
gene oph, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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
into the pETYSBLIC vector for expression in Escherichia coli BL21DE3 cells
Q8YNV6
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)
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
Sphingopyxis sp. M19
-
the enzyme has practical application in ameliorating plastic pollution and protecting the environment
industry
molecular biology
industry
-
oxidized polyvinyl alcohol hydrolase, OPH, is a key enzyme in the degradation of PVA and might have a great potential for application in textile desizing processes
industry
the improved catalytic efficiency of OPH expressed in recombinant Pichia pastoris makes it favorable for industrial applications
molecular biology
-
exhibits 63% identity with OPH of Pseudomonas sp. strain VM15C and 29-32% identity with the polyhydroxybutyrate depolymerases from Mesorhizobium loti, Rhizobium sp. and Sinorhizobium meliloti
molecular biology
-
exhibits 63% identity with OPH of Pseudomonas sp. strain VM15C and 29-32% identity with the polyhydroxybutyrate depolymerases from Mesorhizobium loti, Rhizobium sp. and Sinorhizobium meliloti
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakai, K.; Hamada, N.; Watanabe, Y.
Degradation mechanism of poly(vinyl alcohol) by successive reactions of secondary alcohol oxidase and beta-diketone hydrolase from Pseudomonas sp.
Agric. Biol. Chem.
50
989-996
1986
Pseudomonas sp., Pseudomonas sp. VM15C
-
brenda
Sakai, K.; Hamada, N.; Watanabe, Y.
A new enzyme, beta-diketone hydrolase, a component of a poly(vinyl alcohol)-degrading enzyme preparation
Agric. Biol. Chem.
49
1901-1902
1985
Pseudomonas sp., Pseudomonas sp. VM15C
-
brenda
Shimao, M.; Tamogami, T.; Kishida, S.; Harayama, S.
The gene pvaB encodes oxidized polyvinyl alcohol hydrolase of Pseudomonas sp. strain VM15C and forms an operon with the polyvinyl alcohol dehydrogenase gene pvaA
Microbiology
146
649-657
2000
Pseudomonas sp., Pseudomonas sp. VM15C
brenda
Grogan, G.
Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage
Biochem. J.
388
721-730
2005
Pseudomonas sp., Pseudomonas sp. VM15C
brenda
Klomklang, W.; Tani, A.; Kimbara, K.; Mamoto, R.; Ueda, T.; Shimao, M.; Kawai, F.
Biochemical and molecular characterization of a periplasmic hydrolase for oxidized polyvinyl alcohol from Sphingomonas sp. strain 113P3
Microbiology
151
1255-1262
2005
Sphingomonas sp., Sphingomonas sp. 113P3
brenda
Bennett, J.P.; Whittingham, J.L.; Brzozowski, A.M.; Leonard, P.M.; Grogan, G.
Structural characterization of a beta-diketone hydrolase from the cyanobacterium Anabaena sp. PCC 7120 in native and product-bound forms, a coenzyme A-independent member of the crotonase suprafamily
Biochemistry
46
137-144
2007
Nostoc sp. PCC 7120 = FACHB-418 (Q8YNV6)
brenda
Yang, Y.; Zhang, D.; Liu, S.; Jia, D.; Du, G.; Chen, J.
Expression and fermentation optimization of oxidized polyvinyl alcohol hydrolase in E. coli
J. Ind. Microbiol. Biotechnol.
39
99-104
2012
Sphingopyxis sp.
brenda
Li, M.; Zhang, D.; Du, G.; Chen, J.
Enhancement of PVA-degrading enzyme production by the application of pH control strategy
J. Microbiol. Biotechnol.
22
220-225
2012
Pseudomonas sp., Pseudomonas sp. 113P3, Pseudomonas sp. VM15C
brenda
Yang, Y.; Ko, T.P.; Liu, L.; Li, J.; Huang, C.H.; Chen, J.; Guo, R.T.; Du, G.
Roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase
Biochem. Biophys. Res. Commun.
452
509-514
2014
Pseudomonas sp. (Q9LCQ7), Pseudomonas sp., Pseudomonas sp. VM15C (Q9LCQ7), Sphingopyxis sp. (Q588Z2)
brenda
Yang, Y.; Liu, L.; Li, J.; Du, G.; Chen, J.
Biochemical characterization and high-level production of oxidized polyvinyl alcohol hydrolase from Sphingopyxis sp. 113P3 expressed in methylotrophic Pichia pastoris
Bioprocess Biosyst. Eng.
37
777-782
2014
Sphingopyxis sp. (Q588Z2)
brenda
Yang, Y.; Ko, T.P.; Liu, L.; Li, J.; Huang, C.H.; Chan, H.C.; Ren, F.; Jia, D.; Wang, A.H.; Guo, R.T.; Chen, J.; Du, G.
Structural insights into enzymatic degradation of oxidized polyvinyl alcohol
ChemBioChem
15
1882-1886
2014
Pseudomonas sp. (Q9LCQ7), Pseudomonas sp., Pseudomonas sp. VM15C (Q9LCQ7), Sphingopyxis sp. (Q588Z2)
brenda
Chen, J.; Wang, J.; Li, Y.; Wang, X.; Zhuang, T.; Zhang, Q.; Wang, W.
Catalysis mechanism of oxidized polyvinyl alcohol by pseudomonas hydrolase Insights from molecular dynamics and QM/MM analysis
Chem. Phys. Lett.
721
49-56
2019
Pseudomonas sp. (Q9LCQ7)
-
brenda
Ben Halima, N.
Poly(vinyl alcohol) Review of its promising applications and insights into biodegradation
RSC Adv.
6
39823-39832
2016
Sphingopyxis sp. 113P3 (Q588Z2)
-
brenda
Liu, X.; Wang, D.; Yin, Z.; Sun, L.; Pang, S.; Liu, J.; Li, W.; Cui, S.; Huang, W.; Du, Y.; Xie, Z.
Insights into evolutionary, genomic, and biogeographic characterizations of Chryseobacterium nepalense represented by a polyvinyl alcohol-degrading bacterium, AC3
Microbiol. Spectr.
10
e0217922
2022
Chryseobacterium nepalense, Chryseobacterium nepalense AC3
brenda
Wang, X.; Li, J.; Lin, X.; Zhang, Y.
The s-oph enzyme for efficient degradation of polyvinyl alcohol soluble expression and catalytic properties
Mol. Biol. Rep.
50
8523-8535
2023
Sphingopyxis sp. M19
brenda
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