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 (2017), Eur. Biophys. J., 47, 205-223.

Crystallization (Commentary)

Crystallization (Comment)	Organism
the resonance Raman modes of the oxidized and two-electron reduced 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. They indicate minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center	Enterococcus faecalis

Crystallization (Comment)

Organism

the resonance Raman modes of the oxidized and two-electron reduced 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. They indicate minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center

Enterococcus faecalis

Organism

Organism	UniProt	Comment	Textmining
Enterococcus faecalis	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
commercial preparation	-	Enterococcus faecalis	-

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Enterococcus faecalis

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Release 2023.1 (January 2023)