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Literature summary for 4.1.1.5 extracted from

  • Ji, F.; Li, M.; Feng, Y.; Wu, S.; Wang, T.; Pu, Z.; Wang, J.; Yang, Y.; Xue, S.; Bao, Y.
    Structural and enzymatic characterization of acetolactate decarboxylase from Bacillus subtilis (2018), Appl. Microbiol. Biotechnol., 102, 6479-6491 .
    View publication on PubMed
Search for more literature for 4.1.1.5

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ about 20% residual activity at 1 mM Bacillus subtilis
Fe2+ about 60% residual activity at 1 mM Bacillus subtilis
Mn2+ about 70% residual activity at 1 mM Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
21
-
 DL-2-hydroxy-2-methyl-3-oxobutanoate at pH 6.0 and 30°C Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ about 110% activity at 1 mM Bacillus subtilis
Ca2+ about 160% activity at 1 mM Bacillus subtilis
Mg2+ about 120% activity at 1 mM Bacillus subtilis
Zn2+ the enzyme contains a zinc ion and shows about 130% activity at 1 mM Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2R)-2-hydroxy-2-methyl-3-oxobutanoate Bacillus subtilis
-
 (3R)-3-hydroxybutan-2-one + CO2
-
 ?
(2R)-2-hydroxy-2-methyl-3-oxobutanoate Bacillus subtilis 168
-
 (3R)-3-hydroxybutan-2-one + CO2
-
 ?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate Bacillus subtilis best substrate (3R)-3-hydroxybutan-2-one + CO2
-
 ?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate Bacillus subtilis 168 best substrate (3R)-3-hydroxybutan-2-one + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis 168
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap DEAE column chromatography and Superdex 200 gel filtration Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
-
 Bacillus subtilis (3R)-3-hydroxybutan-2-one + CO2
-
 ?
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
-
 Bacillus subtilis 168 (3R)-3-hydroxybutan-2-one + CO2
-
 ?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate best substrate Bacillus subtilis (3R)-3-hydroxybutan-2-one + CO2
-
 ?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate best substrate Bacillus subtilis 168 (3R)-3-hydroxybutan-2-one + CO2
-
 ?
DL-2-hydroxy-2-methyl-3-oxobutanoate
-
 Bacillus subtilis (3R)-3-hydroxybutan-2-one + CO2
-
 ?
DL-2-hydroxy-2-methyl-3-oxobutanoate
-
 Bacillus subtilis 168 (3R)-3-hydroxybutan-2-one + CO2
-
 ?

Subunits

Subunits Comment Organism
? x * 28799, calculated from amino acid sequence Bacillus subtilis
? x * 28983, MALDI-TOF mass spectrometry Bacillus subtilis

Synonyms

Synonyms Comment Organism
ALDC
-
 Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.2
-
 DL-2-hydroxy-2-methyl-3-oxobutanoate at pH 6.0 and 30°C Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Bacillus subtilis

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.5 8.5 the enzyme activityremains stable between pH 4.5 and 8.5 Bacillus subtilis