Literature summary for 1.4.1.9 extracted from

Zhang, Y.; Wang, Y.; Wang, S.; Fang, B.
Engineering bi-functional enzyme complex of formate dehydrogenase and leucine dehydrogenase by peptide linker mediated fusion for accelerating cofactor regeneration (2017), Eng. Life Sci., 17, 989-996 .

No PubMed abstract available

Application

Application	Comment	Organism
drug development	construction of bifunctional formate dehydrogenase and leucine dehydrogenase enzymatic complex for efficient cofactor regeneration and L-tert leucine biotransformation. L-tert leucine is a widely used chiral building block in many asymmetric reactions for the synthesis of anti-tumor and anti-HIV drugs	Bacillus cereus

Cloned(Commentary)

Cloned (Comment)	Organism
a series of bifunctional enzyme complexes are produced by fusing leucine dehydrogenase and formate dehydrogenase with different peptide linkers, which are expressed in Escherichia coli, purified, and exhibit varied parental enzyme activities and varied L-tert leucine catalytic efficiency. The enzymatic reaction system for L-tert-leucine production and cofactor regeneration with suitable peptide linker is potentially more excellent than free enzymes with lower labor-cost on purification, better thermal stability and higher catalytic efficiency compared with the free coupling of parental enzymes	Bacillus cereus

Cloned (Comment)

Organism

a series of bifunctional enzyme complexes are produced by fusing leucine dehydrogenase and formate dehydrogenase with different peptide linkers, which are expressed in Escherichia coli, purified, and exhibit varied parental enzyme activities and varied L-tert leucine catalytic efficiency. The enzymatic reaction system for L-tert-leucine production and cofactor regeneration with suitable peptide linker is potentially more excellent than free enzymes with lower labor-cost on purification, better thermal stability and higher catalytic efficiency compared with the free coupling of parental enzymes

Bacillus cereus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.0223	-	NADH	pH 10.0, 30°C, fusion enzyme F-S1_L	Bacillus cereus
0.0279	-	NADH	pH 10.0, 30°C, fusion enzyme F-R3-L	Bacillus cereus
0.0349	-	NADH	pH 10.0, 30°C, fusion enzyme F-S3-L	Bacillus cereus
0.0415	-	NADH	pH 10.0, 30°C, fusion enzyme F-DL-L	Bacillus cereus
0.0436	-	NADH	pH 10.0, 30°C, fusion enzyme F-R2-L	Bacillus cereus
0.051	-	NADH	pH 10.0, 30°C, fusion enzyme F-R1-L	Bacillus cereus
0.0605	-	NADH	pH 10.0, 30°C, wild-type enzyme	Bacillus cereus
0.151	-	NADH	pH 10.0, 30°C, fusion enzyme F-S2_L	Bacillus cereus

Organism

Organism	UniProt	Comment	Textmining
Bacillus cereus	Q731C9	-	-
Bacillus cereus ATCC 10987	Q731C9	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bacillus cereus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
trimethylpyruvate + NH3 + NADH + H+	-	Bacillus cereus	L-tert-leucine + H2O + NAD+	-	?
trimethylpyruvate + NH3 + NADH + H+	-	Bacillus cereus ATCC 10987	L-tert-leucine + H2O + NAD+	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Bacillus cereus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
10	-	assay at	Bacillus cereus