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Literature summary for 1.1.2.6 extracted from

  • Hirota-Mamoto, R.; Nagai, R.; Tachibana, S.; Yasuda, M.; Tani, A.; Kimbara, K.; Kawai, F.
    Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase (2006), Microbiology, 152, 1941-1949.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant PVADH tagged with hexahistidine is expressed in Escherichia coli. The three genes encoding oxidized polyvinyl alcohol hydrolase (EC 3.7.1.7), poly(vinyl alcohol) dehydrogenase and cytochrome c are expressed constitutively and form an operon Sphingopyxis sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Sphingopyxis sp.
-
-

Organism

Organism UniProt Comment Textmining
Sphingopyxis sp. Q588Z1
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Sphingopyxis sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
18
-
-
Sphingopyxis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
polyvinyl alcohol + oxidized 2,6-dichlorophenolindophenol polyvinyl alcohol(117) Sphingopyxis sp. polyvinyl alcohol containing oxo-groups + reduced 2,6-dichlorophenolindophenol
-
?

Synonyms

Synonyms Comment Organism
poly(vinyl alcohol) dehydrogenase
-
Sphingopyxis sp.
PVA dehydrogenase
-
Sphingopyxis sp.
pvaA
-
Sphingopyxis sp.
PVADH
-
Sphingopyxis sp.

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Sphingopyxis sp.

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone
-
Sphingopyxis sp.