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Literature summary for 3.7.1.7 extracted from

  • 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 (2014), Bioprocess Biosyst. Eng., 37, 777-782.
    View publication on PubMed

Application

Application Comment Organism
industry the improved catalytic efficiency of OPH expressed in recombinant Pichia pastoris makes it favorable for industrial applications Sphingopyxis sp.

Cloned(Commentary)

Cloned (Comment) Organism
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 Sphingopyxis sp.

Inhibitors

Inhibitors Comment Organism Structure
Ba2+ slight inhibition at 1 mM Sphingopyxis sp.
Ca2+ slight inhibition at 1 mM Sphingopyxis sp.
Co2+ slight inhibition at 1 mM Sphingopyxis sp.
Cr2+ moderate inhibition at 1 mM Sphingopyxis sp.
Cu2+ slight inhibition at 1 mM Sphingopyxis sp.
Fe2+ moderate inhibition at 1 mM Sphingopyxis sp.
Hg2+ strong inhibition at 1 mM Sphingopyxis sp.
phenylmethanesulfonyl fluoride strong inhibition Sphingopyxis sp.
Sn2+ slight inhibition at 1 mM Sphingopyxis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics of the recombinant enzyme with 4-nitrophenyl acetate as substrate Sphingopyxis sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ stimulates the enzyme at 1 mM Sphingopyxis sp.

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sphingopyxis sp. Q588Z2 gene oph
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme 1-67fold from Pichia pastoris strain GS115 culture supernatant by ultrafiltration, and hydrophobic interaction and cation exchange chromatography Sphingopyxis sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
598
-
purified recombinant enzyme, substrate 4-nitrophenyl acetate, pH 8.0, 45°C Sphingopyxis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxidized polyvinyl alcohol + H2O
-
Sphingopyxis sp. ?
-
?

Synonyms

Synonyms Comment Organism
OPH
-
Sphingopyxis sp.
oxidized polyvinyl alcohol hydrolase
-
Sphingopyxis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
recombinant enzyme Sphingopyxis sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
recombinant enzyme, stable up to Sphingopyxis sp.
47.5
-
recombinant enzyme, half-life is 5 h Sphingopyxis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
recombinant enzyme Sphingopyxis sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
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 Sphingopyxis sp.

General Information

General Information Comment Organism
physiological function the enzyme is involved in degradation of polyvinyl alcohol Sphingopyxis sp.