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

BRENDA support

Literature summary for 1.8.1.16 extracted from

  • van Petegem, F.; de Vos, D.; Savvides, S.; Vergauwen, B.; van Beeumen, J.
    Understanding nicotinamide dinucleotide cofactor and substrate specificity in class I flavoprotein disulfide oxidoreductases: crystallographic analysis of a glutathione amide reductase (2007), J. Mol. Biol., 374, 883-999.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the the enzyme both alone and in complex with NAD+ at 2.1 and 2.5 A resolution, respectively Marichromatium gracile

Organism

Organism UniProt Comment Textmining
Marichromatium gracile
-
-
-

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme forms a dimer, with each monomer consisting of a FAD domain, a Rossmann fold NADH binding domain, and an interface domain Marichromatium gracile
NAD+ the enzyme forms a dimer, with each monomer consisting of a FAD domain, a Rossmann fold NADH binding domain, and an interface domain Marichromatium gracile