Literature summary for 1.6.3.4 extracted from

Zhang, Y.W.; Tiwari, M.K.; Gao, H.; Dhiman, S.S.; Jeya, M.; Lee, J.K.
Cloning and characterization of a thermostable H2O-forming NADH oxidase from Lactobacillus rhamnosus (2012), Enzyme Microb. Technol., 50, 255-262.

Search for more literature for 1.6.3.4

Cloned(Commentary)

Cloned (Comment)	Organism
overexpressed in Escherichia coli BL21(DE3)	Lacticaseibacillus rhamnosus

Protein Variants

Protein Variants	Comment	Organism
C42A	produces H2O2, 90% loss of NADH oxidase activity	Lacticaseibacillus rhamnosus

Inhibitors

Inhibitors	Comment	Organism	Structure
Co2+	1 mM, 79% inhibition	Lacticaseibacillus rhamnosus
FAD	optimum FAD concentration for the LrNox is 0.01 mM, with 90% and 3% of maximum activity at 0.001 mM and 0.5 mM FAD, respectively. Enzyme activity decreases sharply with an increase in FAD concentration due to inhibition by FAD. More than 90% enzyme activity is lost when FAD concentration is increased from 0.01 to 0.3 mM	Lacticaseibacillus rhamnosus
Hg2+	1 mM, 85% inhibition	Lacticaseibacillus rhamnosus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0058	-	NADH	pH 5.6, 65°C	Lacticaseibacillus rhamnosus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
50000	-	2 * 50000, SDS-PAGE	Lacticaseibacillus rhamnosus
100000	-	gel filtration	Lacticaseibacillus rhamnosus

Organism

Organism	UniProt	Comment	Textmining
Lacticaseibacillus rhamnosus	-	-	-
Lacticaseibacillus rhamnosus ATCC 53103	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Lacticaseibacillus rhamnosus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 NADH + H+ + O2	-	Lacticaseibacillus rhamnosus	NAD+ + 2 H2O	-	?
2 NADH + H+ + O2	-	Lacticaseibacillus rhamnosus ATCC 53103	NAD+ + 2 H2O	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 50000, SDS-PAGE	Lacticaseibacillus rhamnosus

Synonyms

Synonyms	Comment	Organism
H2O-forming NADH oxidase	-	Lacticaseibacillus rhamnosus
LrNox	-	Lacticaseibacillus rhamnosus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
65	-	-	Lacticaseibacillus rhamnosus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
25	70	the enzyme is not thermal-sensitive since there is an activity change of only 28% when the temperature varies in the range of 25°C to 70°C	Lacticaseibacillus rhamnosus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
30	-	half-life: 55 h	Lacticaseibacillus rhamnosus
40	-	half-life: 33 h	Lacticaseibacillus rhamnosus
50	-	half-life: 14 h	Lacticaseibacillus rhamnosus
60	-	half-life: 6.8 h	Lacticaseibacillus rhamnosus
70	-	half-life: 4.2 h	Lacticaseibacillus rhamnosus
80	-	half-life: 2.1 h	Lacticaseibacillus rhamnosus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.6	-	-	Lacticaseibacillus rhamnosus
7	-	assay at	Lacticaseibacillus rhamnosus

pH Range

pH Minimum	pH Maximum	Comment	Organism
4.6	6	pH 4.6: 68% of maximal activity, pH 6.0: 54% of maximal activity	Lacticaseibacillus rhamnosus

Cofactor

Cofactor	Comment	Organism	Structure
FAD	flavoenzyme. Optimum FAD concentration for the LrNox is 0.01 mM, with 90% and 3% of maximum activity at 0.001 mM and 0.5 mM FAD, respectively. Enzyme activity decreases sharply with an increase in FAD concentration due to inhibition by FAD. More than 90% enzyme activity is lost when FAD concentration is increased from 0.01 to 0.3 mM	Lacticaseibacillus rhamnosus

pI Value

Organism	Comment	pI Value Maximum	pI Value
Lacticaseibacillus rhamnosus	isoelectric focusing	-	5

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
37700	-	NADH	pH 5.6, 65°C	Lacticaseibacillus rhamnosus

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Release 2023.1 (January 2023)