Literature summary 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.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.6.3.1	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
1.6.3.1	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

EC Number	Organism	UniProt	Comment	Textmining
1.6.3.1	Fructilactobacillus sanfranciscensis	-	-	-
1.6.3.1	Lactococcus lactis	-	-	-

Subunits

EC Number	Subunits	Comment	Organism
1.6.3.1	dimer	crystallization data	Fructilactobacillus sanfranciscensis

Cofactor

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

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Release 2023.1 (January 2023)