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Literature summary for 1.1.1.76 extracted from

  • Xu, G.C.; Bian, Y.Q.; Han, R.Z.; Dong, J.J.; Ni, Y.
    Cloning, expression, and characterization of budC gene encoding meso-2,3-butanediol dehydrogenase from Bacillus licheniformis (2016), Appl. Biochem. Biotechnol., 178, 604-617.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Bacillus licheniformis

Inhibitors

Inhibitors Comment Organism Structure
Ag+ strong inhibition Bacillus licheniformis
Al3+ strong inhibition Bacillus licheniformis
Cu2+ strong inhibition Bacillus licheniformis
Fe3+ strong inhibition Bacillus licheniformis
K+ slight inhibition Bacillus licheniformis
additional information not inhibited by EDTA Bacillus licheniformis
Zn2+ slight inhibition Bacillus licheniformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.47
-
(2S)-acetoin at pH 10.0 and 30°C Bacillus licheniformis
7.25
-
(R,R)-butane-2,3-diol at pH 10.0 and 30°C Bacillus licheniformis
72.4
-
diacetyl at pH 5.0 and 30°C Bacillus licheniformis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ slight activation Bacillus licheniformis
Mn2+ slight activation Bacillus licheniformis
additional information not influenced by Ni2+, Ba2+, Li+, Ca2+, and Na+ Bacillus licheniformis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
4 * 30000, SDS-PAGE Bacillus licheniformis
125000
-
gel filtration Bacillus licheniformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2S,3S)-butane-2,3-diol + NAD+ Bacillus licheniformis 100% activity (2S)-acetoin + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography and Superdex 200 gel filtration Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2S)-acetoin + NADH + H+ 97% activity compared to diacetyl Bacillus licheniformis (2S,3S)-butane-2,3-diol + NAD+
-
r
(2S,3S)-butane-2,3-diol + NAD+ 100% activity Bacillus licheniformis (2S)-acetoin + NADH + H+
-
r
(R,R)-butane-2,3-diol + NAD+
-
Bacillus licheniformis ?
-
?
1,2-propanediol + NAD+ 0.57% activity compared to (2S,3S)-butane-2,3-diol Bacillus licheniformis ?
-
?
2,3-hexanedione + NADH + H+ 66% activity compared to diacetyl Bacillus licheniformis ?
-
?
2,3-pentanedione + NADH + H+ 69% activity compared to diacetyl Bacillus licheniformis ?
-
?
3,4-hexanedione + NADH + H+ 10% activity compared to diacetyl Bacillus licheniformis ?
-
?
diacetyl + NADH + H+ 100% activity Bacillus licheniformis (2S)-acetoin + NAD+
-
?
additional information the enzyme shows no activity toward racemic acetoin in the presence of NAD+ as well as no activity with NADPH, 1,4-butanediol, 2,5-hexanedione, 2,4-pentanedione, 2-butanone, methanol, mannitol, and glycerol Bacillus licheniformis ?
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 30000, SDS-PAGE Bacillus licheniformis

Synonyms

Synonyms Comment Organism
BDH
-
Bacillus licheniformis
budC
-
Bacillus licheniformis
meso-2,3-butanediol dehydrogenase
-
Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Bacillus licheniformis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
at 50°C, the enzymatic activity drops rapidly to half of its initial activity within 40 min, then further decreases to 20% after 330 min Bacillus licheniformis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
202
-
(2S)-acetoin at pH 10.0 and 30°C Bacillus licheniformis
591
-
(R,R)-butane-2,3-diol at pH 10.0 and 30°C Bacillus licheniformis
1222
-
diacetyl at pH 5.0 and 30°C Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
for diacetyl reduction Bacillus licheniformis
10
-
for 2,3-butanediol oxidation Bacillus licheniformis

pH Range

pH Minimum pH Maximum Comment Organism
4.5 10 the enzyme shows a relatively high activity over a wide pH range from 5.0 to 8.0 for racemic acetoin reduction and more than 60% of activity is retained between pH 4.5 and 10.0 Bacillus licheniformis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Bacillus licheniformis
NADH
-
Bacillus licheniformis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
16.9
-
diacetyl at pH 5.0 and 30°C Bacillus licheniformis
81.5
-
(R,R)-butane-2,3-diol at pH 10.0 and 30°C Bacillus licheniformis
432
-
(2S)-acetoin at pH 10.0 and 30°C Bacillus licheniformis