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

BRENDA support

Literature summary extracted from

  • Yeom, J.; Park, W.
    Biochemical characterization of ferredoxin-NADP(+) reductase interaction with flavodoxin in Pseudomonas putida (2012), BMB Rep., 45, 476-481.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.18.1.2 homology modeling of wild-type and mutants K259A, K259D. In the wild-type, the Lys259 residue is located close to the FAD cofactor. Lys258 makes van der Waals contacts to the ribose of FAD Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.2 K259A 50% decrease in catalytic efficiency compared to wild-type Pseudomonas putida
1.18.1.2 K259D 50% decrease in catalytic efficiency compared to wild-type Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Pseudomonas putida A0A166IXY4
-
-
1.18.1.2 Pseudomonas putida NBRC 14164 A0A166IXY4
-
-

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 FprA
-
 Pseudomonas putida
1.18.1.2 PP4_41290 ORF name Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD
-
 Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.18.1.2 physiological function Phe256, which is important for binding to ferredoxin, and Lys259 are the crucial residues for electron transfer with ferredoxin Pseudomonas putida