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Literature summary for 1.1.1.304 extracted from

  • Li, J.; Huang, Y.; Chen, X.; Du, Q.; Meng, J.; Xie, N.; Huang, R.
    Enhanced production of optical (S)-acetoin by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration (2018), RSC Adv., 8, 30512-30519 .
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Cloned(Commentary)

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Klebsiella pneumoniae D7RP28
-
-
Mycobacterium sp. B-009 W8VSK8
-
-
Paenibacillus polymyxa A0A5B8J1I7
-
-
Rhodococcus erythropolis M4N626
-
-
Rhodococcus erythropolis WZ010 M4N626
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Klebsiella pneumoniae

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Subunits Comment Organism
? x * 28000, recombinant His-tagged enzyme, SDS-PAGE Klebsiella pneumoniae

Synonyms

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

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

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