Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae | Rhodococcus erythropolis |
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae | Paenibacillus polymyxa |
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae | Mycobacterium sp. B-009 |
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae or glucose dehydrogenase (GDH) gene gdh from Bacillus subtilis | Klebsiella pneumoniae |
Protein Variants | Comment | Organism |
---|---|---|
additional information | acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. Enhanced production of optical (S)-acetoin is achieved by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration. Development of a systematic approach using in situ-NADH regeneration systems and diacetyl reductase. 52.9 g/l of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g/l/h are obtained, production of (S)-acetoin can be effectively improved through the engineering of cofactor regeneration with diacetyl reductase and Gdh or Fdh | Paenibacillus polymyxa |
additional information | acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. Enhanced production of optical (S)-acetoin is achieved by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration. Development of a systematic approach using in situ-NADH regeneration systems and the and diacetyl reductase. 52.9 g/l of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g/l/h are obtained, production of (S)-acetoin can be effectively improved through the engineering of cofactor regeneration with diacetyl reductase and Gdh or Fdh | Rhodococcus erythropolis |
additional information | acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. Enhanced production of optical (S)-acetoin is achieved by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration. Development of a systematic approach using in situ-NADH regeneration systems and the and diacetyl reductase. 52.9 g/l of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g/l/h are obtained, production of (S)-acetoin can be effectively improved through the engineering of cofactor regeneration with diacetyl reductase and Gdh or Fdh | Klebsiella pneumoniae |
additional information | acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. Enhanced production of optical (S)-acetoin is achieved by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration. Development of a systematic approach using in situ-NADH regeneration systems and the and diacetyl reductase. 52.9 g/l of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g/l/h are obtained, production of (S)-acetoin can be effectively improved through the engineering of cofactor regeneration with diacetyl reductase and Gdh or Fdh | Mycobacterium sp. B-009 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
diacetyl + NADH + H+ | Rhodococcus erythropolis | - |
(S)-acetoin + NAD+ | - |
? | |
diacetyl + NADH + H+ | Klebsiella pneumoniae | - |
(S)-acetoin + NAD+ | - |
r | |
diacetyl + NADH + H+ | Paenibacillus polymyxa | - |
(S)-acetoin + NAD+ | - |
? | |
diacetyl + NADH + H+ | Mycobacterium sp. B-009 | - |
(S)-acetoin + NAD+ | - |
? | |
diacetyl + NADH + H+ | Rhodococcus erythropolis WZ010 | - |
(S)-acetoin + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella pneumoniae | D7RP28 | - |
- |
Mycobacterium sp. B-009 | W8VSK8 | - |
- |
Paenibacillus polymyxa | A0A5B8J1I7 | - |
- |
Rhodococcus erythropolis | M4N626 | - |
- |
Rhodococcus erythropolis WZ010 | M4N626 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Klebsiella pneumoniae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
79 | - |
pH 6.5, temperature not specified in the publication, with FDH | Klebsiella pneumoniae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
diacetyl + NADH + H+ | - |
Rhodococcus erythropolis | (S)-acetoin + NAD+ | - |
? | |
diacetyl + NADH + H+ | - |
Klebsiella pneumoniae | (S)-acetoin + NAD+ | - |
r | |
diacetyl + NADH + H+ | - |
Paenibacillus polymyxa | (S)-acetoin + NAD+ | - |
? | |
diacetyl + NADH + H+ | - |
Mycobacterium sp. B-009 | (S)-acetoin + NAD+ | - |
? | |
diacetyl + NADH + H+ | - |
Rhodococcus erythropolis WZ010 | (S)-acetoin + NAD+ | - |
? | |
additional information | KpDAR has clear activities towards diacetyl, (R)/(S)-acetoin (cf. EC 1.1.1.303) and meso-2,3-butanediol with NADH/NAD+ as the cofactor. Diacetyl is the best substrate in the ketone reduction reactions. meso-2,3-Butanediol is the best substrate in the alcohol oxidation reactions, while very low activity is observed with (R)/(S)-acetoin, (2S,3S)-2,3-butanediol (EC 1.1.1.76) and (2R,3R)-2,3-butanediol (EC 1.1.1.4). Optimization of the reaction conditions, overview. Chiral-column GC analyses of products produced by whole-cells of recombinant Escherichia coli | Klebsiella pneumoniae | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
? | x * 28000, recombinant His-tagged enzyme, SDS-PAGE | Klebsiella pneumoniae |
Synonyms | Comment | Organism |
---|---|---|
ADH | - |
Mycobacterium sp. B-009 |
AdR | - |
Rhodococcus erythropolis |
ADS1 | - |
Mycobacterium sp. B-009 |
ardII | - |
Klebsiella pneumoniae |
budC | gene name, UniProt | Klebsiella pneumoniae |
DAR | - |
Rhodococcus erythropolis |
DAR | - |
Klebsiella pneumoniae |
DAR | - |
Paenibacillus polymyxa |
DAR | - |
Mycobacterium sp. B-009 |
diacetyl reductase | - |
Rhodococcus erythropolis |
diacetyl reductase | - |
Klebsiella pneumoniae |
diacetyl reductase | - |
Paenibacillus polymyxa |
diacetyl reductase | - |
Mycobacterium sp. B-009 |
FQU75_06005 | gene name, UniProt | Paenibacillus polymyxa |
Kpdar | - |
Klebsiella pneumoniae |
Ppdar | - |
Paenibacillus polymyxa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Rhodococcus erythropolis |
6.5 | - |
assay at | Klebsiella pneumoniae |
6.5 | - |
assay at | Paenibacillus polymyxa |
6.5 | - |
assay at | Mycobacterium sp. B-009 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Rhodococcus erythropolis | |
NAD+ | - |
Klebsiella pneumoniae | |
NAD+ | - |
Paenibacillus polymyxa | |
NAD+ | - |
Mycobacterium sp. B-009 | |
NADH | - |
Rhodococcus erythropolis | |
NADH | - |
Klebsiella pneumoniae | |
NADH | - |
Paenibacillus polymyxa | |
NADH | - |
Mycobacterium sp. B-009 |