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

BRENDA support

Literature summary 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

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.2.2 periplasm
-
Pseudomonas sp.
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.17.2.2 Pseudomonas sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.2.2
-
Pseudomonas sp.

Substrates and Products (Substrate)

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

Cofactor

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