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

BRENDA support

Literature summary for 1.6.5.5 extracted from

  • Pan, X.; Zhang, H.; Gao, Y.; Li, M.; Chang, W.
    Crystal structures of Pseudomonas syringae pv. tomato DC3000 quinone oxidoreductase and its complex with NADPH. (2009), Biochem. Biophys. Res. Commun., 390, 597-602.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of zeta-crystallin-like quinone oxidoreductase and its complexes with NADPH determined at 2.4 and 2.01 A resolution Pseudomonas syringae

Organism

Organism UniProt Comment Textmining
Pseudomonas syringae
-
pv. tomato DC3000
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 1,4-benzoquinone + NADPH + H+ weak activity Pseudomonas syringae ? + NADP+
-
?
2 9,10-phenanthrenequinone + NADPH + H+ very strong reduction activity towards large substrates such as 9,10-phenanthrenequinone. The zeta-crystallin-like quinone oxidoreductase catalyzes one-electron reduction of certain quinones to generate semiquinone Pseudomonas syringae 2 9,10-phenanthrenesemiquinone + NADP+
-
?

Subunits

Subunits Comment Organism
dimer PtoQOR forms as a homologous dimer, each monomer containing two domains Pseudomonas syringae

Synonyms

Synonyms Comment Organism
PtoQOR
-
Pseudomonas syringae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Pseudomonas syringae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay Pseudomonas syringae

Cofactor

Cofactor Comment Organism Structure
NADPH NADPH binding causes conformational changes in the structure of the enzyme Pseudomonas syringae