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Literature summary extracted from

  • 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 (2014), ChemBioChem, 15, 1882-1886.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.7.1.7 recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Pseudomonas sp.
3.7.1.7 recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Sphingopyxis sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.7.1.7 S172A site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme Pseudomonas sp.
3.7.1.7 S172C site-directed mutagenesis, the mutant shows less than 10% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme Pseudomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.7.1.7 oxidized polyvinyl alcohol + H2O Pseudomonas sp.
-
 ?
-
 ?
3.7.1.7 oxidized polyvinyl alcohol + H2O Sphingopyxis sp.
-
 ?
-
 ?
3.7.1.7 oxidized polyvinyl alcohol + H2O Pseudomonas sp. VM15C
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.7.1.7 Pseudomonas sp. Q9LCQ7
-
-
3.7.1.7 Pseudomonas sp. VM15C Q9LCQ7
-
-
3.7.1.7 Sphingopyxis sp. Q588Z2 gene oph
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.7.1.7 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 Pseudomonas sp.
a
3.7.1.7 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 Sphingopyxis sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.7.1.7 oxidized polyvinyl alcohol + H2O
-
 Pseudomonas sp. ?
-
 ?
3.7.1.7 oxidized polyvinyl alcohol + H2O
-
 Sphingopyxis sp. ?
-
 ?
3.7.1.7 oxidized polyvinyl alcohol + H2O
-
 Pseudomonas sp. VM15C ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.7.1.7 OPH
-
 Pseudomonas sp.
3.7.1.7 OPH
-
 Sphingopyxis sp.
3.7.1.7 oxidized polyvinyl alcohol hydrolase
-
 Pseudomonas sp.
3.7.1.7 oxidized polyvinyl alcohol hydrolase
-
 Sphingopyxis sp.
3.7.1.7 oxidized PVA hydrolase
-
 Pseudomonas sp.
3.7.1.7 oxidized PVA hydrolase
-
 Sphingopyxis sp.
3.7.1.7 pOPH
-
 Pseudomonas sp.
3.7.1.7 pOPH
-
 Sphingopyxis sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.7.1.7 37
-
 assay at Pseudomonas sp.
3.7.1.7 37
-
 assay at Sphingopyxis sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.7.1.7 8
-
 assay at Pseudomonas sp.
3.7.1.7 8
-
 assay at Sphingopyxis sp.

General Information

EC Number General Information Comment Organism
3.7.1.7 evolution the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site Pseudomonas sp.
3.7.1.7 evolution the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site Sphingopyxis sp.
3.7.1.7 additional information substrate binding and catalysis, enzyme modeling, overview Pseudomonas sp.
3.7.1.7 additional information substrate binding and catalysis, enzyme modeling, overview Sphingopyxis sp.
3.7.1.7 physiological function the enzyme is involved in degradation of polyvinyl alcohol Pseudomonas sp.
3.7.1.7 physiological function the enzyme is involved in degradation of polyvinyl alcohol Sphingopyxis sp.