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nonane-4,6-dione + H2O = pentan-2-one + butanoate
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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1-phenyl-1,3-butanedione + H2O
acetic acid + acetophenone
-
-
-
?
1-phenyl-2,4-butanedione + H2O
acetic acid + 1-phenyl-2-propanone
-
-
-
?
2,4-hexanedione + H2O
acetic acid + 2-butanone
2,4-nonanedione + H2O
acetic acid + 2-heptanone
-
-
-
?
2,4-pentanedione + H2O
acetic acid + acetone
3,5-heptanedione + H2O
propionic acid + 2-butanone
3,5-nonanedione + H2O
propionic acid + 2-hexanone
-
-
-
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
5,7-dodecanedione + H2O
valeric acid + 2-hexanone
-
-
-
?
6,8-tridecanedione + H2O
caproic acid + 2-heptanone
-
-
-
?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
bicyclo[2.2.2]octane-2,6-dione + H2O
[(S)-3-oxocyclohexyl]acetic acid
desymmetrization of bicyclo[2.2.2]octane-2,6-dione
-
-
?
nonane-4,6-dione + H2O
pentan-2-one + butanoate
-
-
-
?
oxidized polyvinyl alcohol + H2O
?
p-nitrophenyl acetate + H2O
?
polyvinyl alcohol + H2O
?
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
additional information
?
-
2,4-hexanedione + H2O
acetic acid + 2-butanone
-
-
-
?
2,4-hexanedione + H2O
acetic acid + 2-butanone
-
-
-
?
2,4-hexanedione + H2O
acetic acid + 2-butanone
-
-
-
?
2,4-pentanedione + H2O
acetic acid + acetone
-
-
-
?
2,4-pentanedione + H2O
acetic acid + acetone
-
-
-
?
2,4-pentanedione + H2O
acetic acid + acetone
-
-
-
?
3,5-heptanedione + H2O
propionic acid + 2-butanone
-
-
-
?
3,5-heptanedione + H2O
propionic acid + 2-butanone
-
-
-
?
3,5-heptanedione + H2O
propionic acid + 2-butanone
-
-
-
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
-
-
-
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
-
-
-
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
-
-
-
-
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
-
-
-
-
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
-
-
-
?
4,6-nonanedione + H2O
butyric acid + 2-pentanone
-
-
-
?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
-
-
-
?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
-
-
-
?
6-methyl-2,4-heptanedione + H2O
acetic acid + 4-methyl-2-pentanone
-
-
-
?
oxidized polyvinyl alcohol + H2O
?
-
-
-
?
oxidized polyvinyl alcohol + H2O
?
-
-
-
-
?
oxidized polyvinyl alcohol + H2O
?
-
-
-
?
oxidized polyvinyl alcohol + H2O
?
-
-
-
-
?
oxidized polyvinyl alcohol + H2O
?
-
-
-
-
?
oxidized polyvinyl alcohol + H2O
?
-
-
-
?
p-nitrophenyl acetate + H2O
?
-
-
-
-
?
p-nitrophenyl acetate + H2O
?
-
-
-
-
?
polyvinyl alcohol + H2O
?
-
-
-
-
?
polyvinyl alcohol + H2O
?
-
-
-
-
?
polyvinyl alcohol + H2O
?
-
-
-
-
?
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
-
-
-
?
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
-
-
-
?
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
-
-
-
?
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
-
-
-
?
polyvinyl alcohol + H2O
carboxylic acid + methyl ketone
-
-
-
?
additional information
?
-
-
no activity towards pentane-2,4-dione
-
-
?
additional information
?
-
the enzyme catalyzes the cleavage of C-C bond in beta-diketone
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of C-C bond in beta-diketone
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
no activity towards pentane-2,4-dione
-
-
?
additional information
?
-
the enzyme catalyzes the cleavage of C-C bond in beta-diketone
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
no activity on monoketones, diketones and esters
-
-
?
additional information
?
-
-
no activity on monoketones, diketones and esters
-
-
?
additional information
?
-
the enzyme catalyzes the cleavage of C-C bond in beta-diketone
-
-
?
additional information
?
-
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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-
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
-
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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metabolism
-
oxidized polyvinyl alcohol hydrolase is a key enzyme in the degradation of polyvinyl alcohol
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
-
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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W255A
site-directed mutagenesis
W255F
site-directed mutagenesis
W255Y
site-directed mutagenesis
W255A
-
site-directed mutagenesis
-
W255Y
-
site-directed mutagenesis
-
C241A/C248A
site-directed mutagenesis, the mutant shows unaltered activity compared to 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
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
-
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
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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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
-
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
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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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
Sphingopyxis sp. (Q588Z2), Pseudomonas sp. (Q9LCQ7), Pseudomonas sp., Pseudomonas sp. VM15C (Q9LCQ7)
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
Sphingopyxis sp. (Q588Z2), Pseudomonas sp. (Q9LCQ7), Pseudomonas sp., Pseudomonas sp. VM15C (Q9LCQ7)
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