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Literature summary extracted from

  • Yu, B.; Sun, J.; Bommareddy, R.R.; Song, L.; Zeng, A.P.
    Novel (2R,3R)-2,3-butanediol dehydrogenase from potential industrial strain Paenibacillus polymyxa ATCC 12321 (2011), Appl. Environ. Microbiol., 77, 4230-4233.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.4 open reading frame (ORF) scaffold99_orf00067, DNA and amino acid sequence determination and analysis, phylogenetic analysis Paenibacillus polymyxa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.4 0.046
-
 NADH pH 8.0, 22°C Paenibacillus polymyxa
1.1.1.4 0.3
-
 (3R,3S)-acetoin pH 8.0, 22°C Paenibacillus polymyxa
1.1.1.4 0.54
-
 NAD+ pH 11.0, 22°C Paenibacillus polymyxa
1.1.1.4 1.76
-
 (2R,3R)-butane-2,3-diol pH 11.0, 22°C Paenibacillus polymyxa
1.1.1.4 5.62
-
 meso-butane-2,3-diol pH 11.0, 22°C Paenibacillus polymyxa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+ Paenibacillus polymyxa Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions (3R,3S)-acetoin + NADH + H+
-
 r
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+ Paenibacillus polymyxa ATCC 12321 Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions (3R,3S)-acetoin + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.4 Paenibacillus polymyxa E7EKB8
-
-
1.1.1.4 Paenibacillus polymyxa ATCC 12321 E7EKB8
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+ Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions Paenibacillus polymyxa (3R,3S)-acetoin + NADH + H+
-
 r
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+ sole product in the reduction reaction, preferred substrate in the oxidation reaction Paenibacillus polymyxa (3R,3S)-acetoin + NADH + H+ preferred substrate in the reduction reaction r
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+ Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions Paenibacillus polymyxa ATCC 12321 (3R,3S)-acetoin + NADH + H+
-
 r
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+ sole product in the reduction reaction, preferred substrate in the oxidation reaction Paenibacillus polymyxa ATCC 12321 (3R,3S)-acetoin + NADH + H+ preferred substrate in the reduction reaction r
1.1.1.4 1,2-pentandiol + NAD+
-
 Paenibacillus polymyxa ? + NADH + H+
-
 r
1.1.1.4 1,2-propandiol + NAD+
-
 Paenibacillus polymyxa ? + NADH + H+
-
 r
1.1.1.4 2-propanol + NAD+
-
 Paenibacillus polymyxa 2-propanone + NADH + H+
-
 r
1.1.1.4 2-propanol + NAD+
-
 Paenibacillus polymyxa ATCC 12321 2-propanone + NADH + H+
-
 r
1.1.1.4 diacetyl + NADH + H+ 91% activity compared to (3R,3S)-acetoin in the reduction reaction, cf. EC 1.1.1.303 Paenibacillus polymyxa acetoin + NAD+
-
 ?
1.1.1.4 diacetyl + NADH + H+ 91% activity compared to (3R,3S)-acetoin in the reduction reaction, cf. EC 1.1.1.303 Paenibacillus polymyxa ATCC 12321 acetoin + NAD+
-
 ?
1.1.1.4 glycerol + NAD+
-
 Paenibacillus polymyxa ? + NADH + H+
-
 r
1.1.1.4 meso-butane-2,3-diol + NAD+ 72% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction Paenibacillus polymyxa acetoin + NADH + H+
-
 r
1.1.1.4 additional information the enzyme is also active in reduction reaction with diacetyl (91% compared to (2R,3S)-acetoin) and glyceraldehyde-3-phosphate (12% compared to (2R,3S)-acetoin), cf. EC 1.1.1.303 and EC 1.1.1.8, respectively, but not with dihydroxyacetone phosphate. It shows low activity in oxidation reaction with ethanol, n-propanol, n-butanol, 1,3-propanediol, and 1,5-pentanediol Paenibacillus polymyxa ?
-
 ?
1.1.1.4 additional information the enzyme is also active in reduction reaction with diacetyl (91% compared to (2R,3S)-acetoin) and glyceraldehyde-3-phosphate (12% compared to (2R,3S)-acetoin), cf. EC 1.1.1.303 and EC 1.1.1.8, respectively, but not with dihydroxyacetone phosphate. It shows low activity in oxidation reaction with ethanol, n-propanol, n-butanol, 1,3-propanediol, and 1,5-pentanediol Paenibacillus polymyxa ATCC 12321 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.4 (2R,3R)-2,3-butanediol dehydrogenase
-
 Paenibacillus polymyxa
1.1.1.4 BDH99::67
-
 Paenibacillus polymyxa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.4 22
-
 assay at room temperature Paenibacillus polymyxa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.4 8
-
 reduction reaction Paenibacillus polymyxa
1.1.1.4 11
-
 oxidation reaction Paenibacillus polymyxa

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.4 NAD+
-
 Paenibacillus polymyxa
1.1.1.4 NADH
-
 Paenibacillus polymyxa

General Information

EC Number General Information Comment Organism
1.1.1.4 evolution the (2R,3R)-2,3-butanediol dehydrogenase belongs to the mostly zinc-containing medium-chain dehydrogenase/reductase superfamily and not to the short-chain dehydrogenase/reductase superfamily, to which meso- and (2S,3S)-2,3-butanediol dehydrogenases belong, phylogenetic analysis. The enzyme contains two hydrophobic residues forming the binding site for cofactor NAD(P), Phe138 and Leu141 (numbers refer to R,R-BDH of Saccharomyces cerevisiae) Paenibacillus polymyxa