Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.5 21
-
 DL-2-hydroxy-2-methyl-3-oxobutanoate at pH 6.0 and 30°C Bacillus subtilis

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.5 (2R)-2-hydroxy-2-methyl-3-oxobutanoate Bacillus subtilis
-
 (3R)-3-hydroxybutan-2-one + CO2
-
 ?
4.1.1.5 (2R)-2-hydroxy-2-methyl-3-oxobutanoate Bacillus subtilis 168
-
 (3R)-3-hydroxybutan-2-one + CO2
-
 ?
4.1.1.5 (2S)-2-hydroxy-2-methyl-3-oxobutanoate Bacillus subtilis best substrate (3R)-3-hydroxybutan-2-one + CO2
-
 ?
4.1.1.5 (2S)-2-hydroxy-2-methyl-3-oxobutanoate Bacillus subtilis 168 best substrate (3R)-3-hydroxybutan-2-one + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.5 Bacillus subtilis
-
-
-
4.1.1.5 Bacillus subtilis 168
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.5 (2R)-2-hydroxy-2-methyl-3-oxobutanoate
-
 Bacillus subtilis (3R)-3-hydroxybutan-2-one + CO2
-
 ?
4.1.1.5 (2R)-2-hydroxy-2-methyl-3-oxobutanoate
-
 Bacillus subtilis 168 (3R)-3-hydroxybutan-2-one + CO2
-
 ?
4.1.1.5 (2S)-2-hydroxy-2-methyl-3-oxobutanoate best substrate Bacillus subtilis (3R)-3-hydroxybutan-2-one + CO2
-
 ?
4.1.1.5 (2S)-2-hydroxy-2-methyl-3-oxobutanoate best substrate Bacillus subtilis 168 (3R)-3-hydroxybutan-2-one + CO2
-
 ?
4.1.1.5 DL-2-hydroxy-2-methyl-3-oxobutanoate
-
 Bacillus subtilis (3R)-3-hydroxybutan-2-one + CO2
-
 ?
4.1.1.5 DL-2-hydroxy-2-methyl-3-oxobutanoate
-
 Bacillus subtilis 168 (3R)-3-hydroxybutan-2-one + CO2
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
4.1.1.5 ALDC
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.5 2.2
-
 DL-2-hydroxy-2-methyl-3-oxobutanoate at pH 6.0 and 30°C Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.5 5
-
-
 Bacillus subtilis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.1.1.5 4.5 8.5 the enzyme activityremains stable between pH 4.5 and 8.5 Bacillus subtilis