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Literature summary 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

EC Number Application Comment Organism
1.4.1.9 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
1.17.1.9 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 [Candida] boidinii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.9 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
1.17.1.9 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 [Candida] boidinii
1.17.1.9 expressed in Escherichia coli BL21(DE3) cells [Candida] boidinii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.9 0.0223
-
 NADH pH 10.0, 30°C, fusion enzyme F-S1_L Bacillus cereus
1.4.1.9 0.0279
-
 NADH pH 10.0, 30°C, fusion enzyme F-R3-L Bacillus cereus
1.4.1.9 0.0349
-
 NADH pH 10.0, 30°C, fusion enzyme F-S3-L Bacillus cereus
1.4.1.9 0.0415
-
 NADH pH 10.0, 30°C, fusion enzyme F-DL-L Bacillus cereus
1.4.1.9 0.0436
-
 NADH pH 10.0, 30°C, fusion enzyme F-R2-L Bacillus cereus
1.4.1.9 0.051
-
 NADH pH 10.0, 30°C, fusion enzyme F-R1-L Bacillus cereus
1.4.1.9 0.0605
-
 NADH pH 10.0, 30°C, wild-type enzyme Bacillus cereus
1.4.1.9 0.151
-
 NADH pH 10.0, 30°C, fusion enzyme F-S2_L Bacillus cereus
1.17.1.9 0.026
-
 NAD+ pH 7.5, 30°C, fusion enzyme F-S3-L [Candida] boidinii
1.17.1.9 0.037
-
 NAD+ pH 7.5, 30°C, fusion enzyme F-R1-L [Candida] boidinii
1.17.1.9 0.039
-
 NAD+ pH 7.5, 30°C, fusion enzyme F-DL-L [Candida] boidinii
1.17.1.9 0.045
-
 NAD+ pH 7.5, 30°C, fusion enzyme F-R3-L [Candida] boidinii
1.17.1.9 0.051
-
 NAD+ pH 7.5, 30°C, fusion enzyme F-R2-L [Candida] boidinii
1.17.1.9 0.052
-
 NAD+ pH 7.5, 30°C, fusion enzyme F-S2-L [Candida] boidinii
1.17.1.9 0.066
-
 NAD+ pH 7.5, 30°C, fusion enzyme F-S1-L [Candida] boidinii
1.17.1.9 0.623
-
 NAD+ pH 7.5, 30°C, wild-type enzyme [Candida] boidinii
1.17.1.9 0.62322
-
 NAD+ at pH 7.5 and 30°C [Candida] boidinii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.1.9 formate + NAD+ [Candida] boidinii
-
 CO2 + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.9 Bacillus cereus Q731C9
-
-
1.4.1.9 Bacillus cereus ATCC 10987 Q731C9
-
-
1.17.1.9 [Candida] boidinii O13437
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.9
-
 Bacillus cereus
1.17.1.9
-
 [Candida] boidinii
1.17.1.9 HisTrap column chromatography [Candida] boidinii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.9 trimethylpyruvate + NH3 + NADH + H+
-
 Bacillus cereus L-tert-leucine + H2O + NAD+
-
 ?
1.4.1.9 trimethylpyruvate + NH3 + NADH + H+
-
 Bacillus cereus ATCC 10987 L-tert-leucine + H2O + NAD+
-
 ?
1.17.1.9 formate + NAD+
-
 [Candida] boidinii CO2 + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.17.1.9 FDH I
-
 [Candida] boidinii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.1.9 30
-
 assay at Bacillus cereus
1.17.1.9 30
-
 assay at [Candida] boidinii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.9 10
-
 assay at Bacillus cereus
1.17.1.9 7.5
-
 assay at [Candida] boidinii

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.9 NAD+
-
 [Candida] boidinii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.17.1.9 70
-
 NAD+ at pH 7.5 and 30°C [Candida] boidinii