Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.2.6 extracted from

  • Mamoto, R.; Hu, X.; Chiue, H.; Fujioka, Y.; Kawai, F.
    Cloning and expression of soluble cytochrome c and its role in polyvinyl alcohol degradation by polyvinyl alcohol-utilizing Sphingopyxis sp. strain 113P3 (2008), J. Biosci. Bioeng., 105, 147-151.
    View publication on PubMed

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
polyvinyl alcohol + ferricytochrome c Sphingopyxis sp. cytochrome c involved in the pva operon is a physiological primary electron acceptor for PVADH polyvinyl alcohol containing oxo-groups + ferrocytochrome c + H+
-
?

Organism

Organism UniProt Comment Textmining
Sphingopyxis sp. Q588Z1 the gene encoding the enzyme is located in the pva operon
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
polyvinyl alcohol + ferricytochrome c cytochrome c involved in the pva operon is a physiological primary electron acceptor for PVADH Sphingopyxis sp. polyvinyl alcohol containing oxo-groups + ferrocytochrome c + H+
-
?
polyvinyl alcohol + ferricytochrome c
-
Sphingopyxis sp. polyvinyl alcohol containing oxo-groups + ferrocytochrome c + 2 H+
-
?

Synonyms

Synonyms Comment Organism
PVA dehydrogenase
-
Sphingopyxis sp.
PVADH
-
Sphingopyxis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Sphingopyxis sp.

Cofactor

Cofactor Comment Organism Structure
cytochrome c cytochrome c involved in the pva operon is a physiological primary electron acceptor for polyvinyl-alcohol dehydrogenase Sphingopyxis sp.

General Information

General Information Comment Organism
physiological function the cytochrome c involved in the pva operon is a physiological primary electron acceptor for PVADH, and PVA dehydrogenation is linked with the respiratory chain in Sphingopyxis sp. strain 113P3 Sphingopyxis sp.