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Literature summary for 1.11.1.1 extracted from

  • Keirsse-Haquin, J.; Picaud, T.; Bordes, L.; de Gracia, A.G.; Desbois, A.
    Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase a resonance Raman study (2018), Eur. Biophys. J., 47, 205-223 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Enterococcus faecalis

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis
-
-
-

Synonyms

Synonyms Comment Organism
Npx
-
Enterococcus faecalis

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein. The resonance Raman (RR) modes of the oxidized and twoelectron reduced (EH2) forms of Npx are related to very tight flavin-protein interactions maintaining a nearly planar conformation of the isoalloxazine tricycle, a low level of H-bonding at the N1/N5 and O2/O4 sites, and a strong H-bond at N3H. Minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center Enterococcus faecalis