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Literature summary for 1.17.2.2 extracted from

  • Hopper, D.J.; Rogozinski, J.
    Redox potential of the haem c group in the quinocytochrome, lupanine hydroxylase, an enzyme located in the periplasm of a Pseudomonas sp. (1998), Biochim. Biophys. Acta, 1383, 160-164.
    View publication on PubMed

Localization

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

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lupanine + pyrroloquinoline quinone + H2O
-
Pseudomonas sp. 17-hydroxylupanine + pyrroloquinoline quinol
-
?

Cofactor

Cofactor Comment Organism Structure
heme the midpoint redox potential of the heme in the purified enzyme is + 193 mV Pseudomonas sp.
pyrroloquinoline quinone removed from the enzyme by isoelectric focusing to give inactive apoenzyme Pseudomonas sp.