Literature summary for 1.6.3.1 extracted from

Lountos, G.T.; Jiang, R.; Wellborn, W.B.; Thaler, T.L.; Bommarius, A.S.; Orville, A.M.
The crystal structure of NAD(P)H oxidase from Lactobacillus sanfranciscensis: insights into the conversion of O2 into two water molecules by the flavoenzyme (2006), Biochemistry, 45, 9648-9659.

Search for more literature for 1.6.3.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme crystallizes as dimer, with each monomer consisting of a FAD-binding domain, a NAD(P)H -binding domain and a dimerization domain. Redox-active C42 is in sulfenic acid state Cys-SOH and shows two conformations, either hydrogen bonded to H10 or hydrogen bonded to FAD O2 atom. The NAD(P)H-binding domains each contain ATP as ligand, being not inhibitory to the enzyme	Fructilactobacillus sanfranciscensis
homology modeling of structure using the crystal structure of Lactobacillus sanfranciscensis. In contrast to Lactobacillus sanfranciscensis, the Lactococcus lactis enzyme does not bind ADP, being consistent with its specificity for NADH	Lactococcus lactis

Organism

Organism	UniProt	Comment	Textmining
Fructilactobacillus sanfranciscensis	-	-	-
Lactococcus lactis	-	-	-

Subunits

Subunits	Comment	Organism
dimer	crystallization data	Fructilactobacillus sanfranciscensis

Cofactor

Cofactor	Comment	Organism	Structure
ADP	bound to NAD(P)H-binding domain	Fructilactobacillus sanfranciscensis
FAD	-	Lactococcus lactis
FAD	-	Fructilactobacillus sanfranciscensis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)