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Literature summary for 4.1.1.5 extracted from

  • Najmudin, S.; Andersen, J.T.; Patkar, S.A.; Borchert, T.V.; Crout, D.H.G.; Fülöp, V.
    Purification, crystallization and preliminary X-ray crystallographic studies on acetolactate decarboxylase (2003), Acta Crystallogr. Sect. D, 59, 1073-1075.
    View publication on PubMed
Search for more literature for 4.1.1.5

Application

Application Comment Organism
nutrition ADC has a practical application in brewing, used to speed maturation Brevibacillus brevis

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Bacillus subtilis JA222 Brevibacillus brevis

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant enzyme, expressed in Bacillus subtilis JA222, hanging drop vapour-diffusion method, X-ray structure Brevibacillus brevis

Organism

Organism UniProt Comment Textmining
Brevibacillus brevis
-
 strain ATCC 11031
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme, expressed in Bacillus subtilis JA222 Brevibacillus brevis

Reaction

Reaction Comment Organism Reaction ID
(2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO2 mechanism Brevibacillus brevis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-2-hydroxy-2-methyl-3-oxobutanoate decarboxylates both enantiomers of acetolactate to form (R)-acetoin, decarboxylation at a lower rate than of the (S)-enantiomer, mechanism Brevibacillus brevis (R)-acetoin + CO2
-
 ?
(S)-2-hydroxy-2-ethyl-3-oxobutanoate
-
 Brevibacillus brevis (R)-3-hydroxypentan-2-one + CO2
-
 ?
(S)-2-hydroxy-2-methyl-3-oxobutanoate decarboxylates both enantiomers of acetolactate to form (R)-acetoin, (S)-enantiomer is the normal substrate, mechanism Brevibacillus brevis (R)-acetoin + CO2
-
 ?

Synonyms

Synonyms Comment Organism
ADC
-
 Brevibacillus brevis

pI Value

Organism Comment pI Value Maximum pI Value
Brevibacillus brevis around
-
 6