Literature summary for 1.5.1.36 extracted from

Man, Z.; Rao, Z.; Xu, M.; Guo, J.; Yang, T.; Zhang, X.; Xu, Z.
Improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply (2016), Metab. Eng., 38, 310-321 .

Search for more literature for 1.5.1.36

Cloned(Commentary)

Cloned (Comment)	Organism
gene frd2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)	Corynebacterium crenatum

Protein Variants

Protein Variants	Comment	Organism
additional information	improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview	Corynebacterium crenatum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0084	-	NADH	with FMN, pH 7.5, 30°C, recombinant enzyme	Corynebacterium crenatum
0.0141	-	NADH	with FAD, pH 7.5, 30°C, recombinant enzyme	Corynebacterium crenatum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
FAD + NAD(P)H	Corynebacterium crenatum	-	FADH2 + NAD(P)+	-	r
FMN + NAD(P)H	Corynebacterium crenatum	-	FMNH2 + NAD(P)+	-	r

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium crenatum	-	-	-
Corynebacterium crenatum SYPA5-5	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Corynebacterium crenatum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
FAD + NAD(P)H	-	Corynebacterium crenatum	FADH2 + NAD(P)+	-	r
FMN + NAD(P)H	-	Corynebacterium crenatum	FMNH2 + NAD(P)+	-	r
FMN + NADH	-	Corynebacterium crenatum	FMNH2 + NAD+	-	r
FMN + NADPH	-	Corynebacterium crenatum	FMNH2 + NADP+	-	r
additional information	the enzyme is also active with FMN and NADPH, cf. EC 1.5.1.30	Corynebacterium crenatum	?	-	?
additional information	the enzyme is also active with FMN and NADPH, cf. EC 1.5.1.30	Corynebacterium crenatum SYPA5-5	?	-	?

Synonyms

Synonyms	Comment	Organism
Frd188	-	Corynebacterium crenatum
frd2	-	Corynebacterium crenatum
NAD(P)H-dependent H2O2-forming flavin reductase	-	Corynebacterium crenatum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Corynebacterium crenatum

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.0247	-	NADH	with FMN, pH 7.5, 30°C, recombinant enzyme	Corynebacterium crenatum
0.0357	-	NADH	with FAD, pH 7.5, 30°C, recombinant enzyme	Corynebacterium crenatum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Corynebacterium crenatum

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Corynebacterium crenatum
NADH	-	Corynebacterium crenatum

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
2.53	-	NADH	with FAD, pH 7.5, 30°C, recombinant enzyme	Corynebacterium crenatum
2.94	-	NADH	with FMN, pH 7.5, 30°C, recombinant enzyme	Corynebacterium crenatum

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)