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Literature summary extracted from

  • Takeda, M.; Muranushi, T.; Inagaki, S.; Nakao, T.; Motomatsu, S.; Suzuki, I.; Koizumi, J.
    Identification and characterization of a mycobacterial (2R,3R)-2,3-butanediol dehydrogenase (2011), Biosci. Biotechnol. Biochem., 75, 2384-2389.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.4 gene mbd1, DNA and amino acid sequence determination and analysis, phylogenetic analysis Mycobacterium sp.
1.1.1.4 phylogenetic analysis Mycolicibacterium smegmatis
1.1.1.4 phylogenetic analysis Mycolicibacterium vanbaalenii
1.1.1.4 phylogenetic analysis Mycolicibacterium gilvum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.4 5,5'-dithiobis(2-nitrobenzoic acid)
-
Mycobacterium sp.
1.1.1.4 Cu2+
-
Mycobacterium sp.
1.1.1.4 EDTA
-
Mycobacterium sp.
1.1.1.4 Hg2+
-
Mycobacterium sp.
1.1.1.4 Zn2+
-
Mycobacterium sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.4 0.06
-
(3R,3S)-acetoin pH 7.0, 30°C Mycobacterium sp.

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+ Mycobacterium sp. preferred substrate (3R,3S)-acetoin + NADH + H+
-
r
1.1.1.4 rac-1,2-propanediol + NAD+ Mycobacterium sp.
-
hydroxyacetone + NADH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.4 Mycobacterium sp. F1T242 gene mbd1
-
1.1.1.4 Mycolicibacterium gilvum
-
-
-
1.1.1.4 Mycolicibacterium smegmatis
-
-
-
1.1.1.4 Mycolicibacterium vanbaalenii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.4 native enzyme by anion exchange and hydrophobic interaction chromatography, followed by ultrafiltration and native PAGE Mycobacterium sp.

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+ preferred substrate Mycobacterium sp. (3R,3S)-acetoin + NADH + H+
-
r
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+ preferred substrate, very low activity with the (S)-enantiomer Mycobacterium sp. (3R,3S)-acetoin + NADH + H+
-
r
1.1.1.4 (R)-1,2-propanediol + NAD+ 73% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction, very low activity with the (S)-enantiomer Mycobacterium sp. hydroxyacetone + NADH + H+
-
?
1.1.1.4 1,2-hexanediol + NAD+ 50% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction Mycobacterium sp. ? + NADH + H+
-
?
1.1.1.4 1,2-pentanediol + NAD+ 74% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction Mycobacterium sp. ? + NADH + H+
-
?
1.1.1.4 meso-butane-2,3-diol + NAD+ 61% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction Mycobacterium sp. acetoin + NADH + H+
-
r
1.1.1.4 additional information substrate specificity, overview. No or poor activity with ethanol, ethylene glycol, diethylene glycol, 1-propanol, 2-propanol, 1,3-propanediol, glycerol, dipropylene glycol, 1-butanol, 1,4-butanediol, 1,2,4-butanetriol, (2S,3S)-butane-2,3-diol, 1,5-pentanediol, 2,4-pentanediol, 3-methyl-1,5-pentandiol, and 1,2,6-hexantriol Mycobacterium sp. ?
-
?
1.1.1.4 rac-1,2-propanediol + NAD+
-
Mycobacterium sp. hydroxyacetone + NADH + H+
-
?
1.1.1.4 rac-1,2-propanediol + NAD+ 68% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction Mycobacterium sp. hydroxyacetone + NADH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.4 ? x * 36430, sequence calculation Mycobacterium sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.1.4 (2R,3R)-2,3-butanediol dehydrogenase
-
Mycolicibacterium smegmatis
1.1.1.4 (2R,3R)-2,3-butanediol dehydrogenase
-
Mycolicibacterium vanbaalenii
1.1.1.4 (2R,3R)-2,3-butanediol dehydrogenase
-
Mycolicibacterium gilvum
1.1.1.4 (2R,3R)-2,3-butanediol dehydrogenase
-
Mycobacterium sp.
1.1.1.4 R,R-BD-DH
-
Mycolicibacterium smegmatis
1.1.1.4 R,R-BD-DH
-
Mycolicibacterium vanbaalenii
1.1.1.4 R,R-BD-DH
-
Mycolicibacterium gilvum
1.1.1.4 R,R-BD-DH
-
Mycobacterium sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.4 85
-
-
Mycobacterium sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.4 50
-
rapid denaturation of the purified enzyme above 50°C Mycobacterium sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.4 7
-
assay at, reduction reaction Mycobacterium sp.
1.1.1.4 7.5
-
assay at, oxidation reaction Mycobacterium sp.

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.4 5 8.5 stable, rapid denaturation below pH 5.0 Mycobacterium sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.4 NAD+
-
Mycobacterium sp.
1.1.1.4 NADH
-
Mycobacterium sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.1.4 Mycobacterium sp. isoelectric focussing
-
4.9

General Information

EC Number General Information Comment Organism
1.1.1.4 evolution the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis Mycolicibacterium smegmatis
1.1.1.4 evolution the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis Mycolicibacterium vanbaalenii
1.1.1.4 evolution the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis Mycolicibacterium gilvum
1.1.1.4 evolution the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis Mycobacterium sp.