Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
(2R,3R)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
transition state analogue acts as substrate and competitive inhibitor
-
-
?
(2R,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
transition state analogue acts as substrate and mixed-type inhibitor
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
(2S,3R)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
transition state analogue acts as substrate and competitive inhibitor
-
-
?
(2S,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
transition state analogue acts as substrate and competitive inhibitor
-
-
?
(2S,3S)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
transition state analogue acts as substrate and competitive inhibitor
-
-
?
(R)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
decarboxylates both enantiomers of acetolactate to form (R)-acetoin, decarboxylation at a lower rate than of the (S)-enantiomer, mechanism
-
?
(S)-2-hydroxy-2-ethyl-3-oxobutanoate
(R)-3-hydroxypentan-2-one + CO2
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
2-Hydroxy-2-ethyl-3-oxobutanoate
3-Hydroxypentan-2-one + CO2
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
2-Hydroxy-2-methyl-3-oxobutanoate
?
alpha-acetolactate + CO2
acetoin
-
-
-
-
?
DL-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
additional information
?
-
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
ir
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
best substrate
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
best substrate
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
ir
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
acetolactate decarboxylase catalyzes the conversion of both enantiomers of acetolactate to the (R)-enantiomer of acetoin, via a mechanism that involves a prior rearrangement of the non-natural (R)-enantiomer substrate to the natural (S)-enantiomer
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
decarboxylates both enantiomers of acetolactate to form (R)-acetoin, (S)-enantiomer is the normal substrate, mechanism
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
alpha-acetolactate metabolism
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
catalyzes the second step of the acetoin pathway, catabolism of pyruvate, responsible for the regulation of the pool of alpha-acetolactate in the cell during branched-chain amino acids metabolism, mode of transcriptional and translational regulation of ALDC production
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
regulates leucine and valine biosynthesis by diverting the flux of alpha-acetolactate towards acetoin when branched-chain amino acids are present at a high concentration, involved in catabolism of pyruvate to acetoin, but less important function in vivo
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
regulates leucine and valine biosynthesis by diverting the flux of alpha-acetolactate towards acetoin when branched-chain amino acids are present at a high concentration, involved in catabolism of pyruvate to acetoin, but less important function in vivo
-
?
2-Hydroxy-2-ethyl-3-oxobutanoate
3-Hydroxypentan-2-one + CO2
Acidobacterium aerogenes
-
specifically decarboxylates the (S)-enantiomer
-
-
?
2-Hydroxy-2-ethyl-3-oxobutanoate
3-Hydroxypentan-2-one + CO2
-
both enantiomers
-
?
2-Hydroxy-2-ethyl-3-oxobutanoate
3-Hydroxypentan-2-one + CO2
-
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
Achromobacter metalcaligenes
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
Acidobacterium aerogenes
-
specifically decarboxylates the S-enantiomer, forming (R)-acetoin with inversion of configuration
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
-
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
?
-
enzyme is a key regulator of Val and Leu biosynthesis, by controlling the acetolactate flux by a shift to catabolism
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
?
-
enzyme catalyzes the second step of the 2,3-butanediol pathway
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
?
-
activation by Leu, Val and Ile
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
?
-
activation by Leu, Val and Ile
-
-
?
2-Hydroxy-2-methyl-3-oxobutanoate
?
-
enzyme is involved in acetoin production
-
-
?
DL-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
DL-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
-
-
-
-
?
additional information
?
-
-
the enzyme in D2O induces a D/H exchange in (R)-acetoin and not the (S)-isomer to give a deuteriated product with retention of configuration
-
-
?
additional information
?
-
-
the enzyme isomerizes (S)-2-acetohydroxybutyrate to (R)-3-hydroxypentan-2-one
-
-
?
additional information
?
-
-
evidence for the putative carboxylate migration during decarboxylation of (R)-isomers of 2-hydroxy-2-methyl-3-oxobutanoate and analogues
-
-
?
additional information
?
-
the enzyme appears to catalyze both the stereoselective decarboxylation/protonation and the rearrangement reaction of the non-natural substrate. The enzyme isomerizes (S)-2-acetohydroxybutyrate to (R)-3-hydroxypentan-2-one and (S)-2-hydroxy-2-methyl-3-oxopentanoate to (R)-2-hydroxypentan-3-one
-
-
?
additional information
?
-
-
pyruvate metabolism
-
?
additional information
?
-
-
ALD does not catalyze the direct production of diacetyl from 2-acetolactate
-
?
additional information
?
-
-
citrate metabolism
-
?
additional information
?
-
-
ALD does not catalyze the direct production of diacetyl from 2-acetolactate
-
?
additional information
?
-
-
citrate metabolism
-
?
additional information
?
-
not: alpha-acetohydroxybutyrate
-
?
additional information
?
-
-
not: alpha-acetohydroxybutyrate
-
?
additional information
?
-
not: alpha-acetohydroxybutyrate
-
?
additional information
?
-
-
not: alpha-acetohydroxybutyrate
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Acetobacter aceti subsp. xylinum
UniProt
brenda
Achromobacter metalcaligenes
1 strain generates the enzyme and 2 strains do not
-
-
brenda
Acidobacterium aerogenes
-
-
-
brenda
-
-
-
brenda
7 strains generate the enzyme and 1 strain does not
-
-
brenda
8 strains generate the enzyme and 5 strains do not
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
2 strains generate the enzyme and 2 strains does not
-
-
brenda
3 strains generate the enzyme and 4 strains do not
-
-
brenda
-
-
-
brenda
2 strains generate the enzyme and 3 strains do not
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
one strain generates the enzyme and another strain does not
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
subsp. cremoris
-
-
brenda
subsp. diacetilactis
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
2 strains generate the enzyme and 1 strain does not
-
-
brenda
-
-
-
brenda
no activity in Acinetobacter sp.
-
-
-
brenda
no activity in Acremonium fusioides
-
-
-
brenda
no activity in Agrobacterium tumefaciens
-
-
-
brenda
no activity in Alcaligenes faecalis
-
-
-
brenda
no activity in Ascodesmis nigricans
-
-
-
brenda
no activity in Ascoidea rubescens
-
-
-
brenda
no activity in Aspergillus clavatus
-
-
-
brenda
no activity in Aspergillus niger
-
-
-
brenda
no activity in Aureobasidium pullulans
-
-
-
brenda
no activity in Bacillus sp.
-
-
-
brenda
no activity in Botrytis allii
-
-
-
brenda
no activity in Brevibacterium divaricatum
-
-
-
brenda
no activity in Byssochlamys fulva
-
-
-
brenda
no activity in Cephalosporium acremonium
-
-
-
brenda
no activity in Cephalosporium spinosum
-
-
-
brenda
no activity in Ceratocystis piceae
-
-
-
brenda
no activity in Chaetomella terricola
-
-
-
brenda
no activity in Chaetomium globosum
-
-
-
brenda
no activity in Chromobacterium violaceum
-
-
-
brenda
no activity in Chrysosporium keratinophilum
-
-
-
brenda
no activity in Citrobacter freundii
-
-
-
brenda
no activity in Clostridium acetobutyricum
-
-
-
brenda
no activity in Clostridium bifermentans
-
-
-
brenda
no activity in Clostridium histolyticum
-
-
-
brenda
no activity in Clostridium innocuum
-
-
-
brenda
no activity in Clostridium perfringens
-
-
-
brenda
no activity in Clostridium propionicum
-
-
-
brenda
no activity in Clostridium sporogenes
-
-
-
brenda
no activity in Coniothyrium carpaticum
-
-
-
brenda
no activity in Cunninghamella blakesleeana
-
-
-
brenda
no activity in Dipodascus aggregatus
-
-
-
brenda
no activity in Emericellopsis salmosynnemata
-
-
-
brenda
no activity in Epicoccum andropogonis
-
-
-
brenda
no activity in Erwinia sp.
-
-
-
brenda
no activity in Escherichia coli
-
-
-
brenda
no activity in Flavobacterium meningosepticum
-
-
-
brenda
no activity in Flavobacterium sp.
-
-
-
brenda
no activity in Fomes annosus
-
-
-
brenda
no activity in Geotrichum candidum
-
-
-
brenda
no activity in Helminthosporium solani
-
-
-
brenda
no activity in Hypomyces solani
-
-
-
brenda
no activity in Klebsiella pneumoniae
-
-
-
brenda
no activity in Kloeckera apiculata
-
-
-
brenda
no activity in Lactobacillus brevis
-
-
-
brenda
no activity in Lactobacillus buchneri
-
-
-
brenda
no activity in Lactobacillus bulgaricus
-
-
-
brenda
no activity in Lactobacillus fermentum
ATCC 9338
-
-
brenda
no activity in Lactobacillus helveticus
-
-
-
brenda
no activity in Lactococcus lactis subsp. lactis bv. diacetylactis strain B2103/74
-
-
-
brenda
no activity in Leuconostoc citrovorum
-
-
-
brenda
no activity in Melanconium juglandinum
-
-
-
brenda
no activity in Micrococcus sp.
-
-
-
brenda
no activity in Monascus ruber
-
-
-
brenda
no activity in Monotospora brevis
-
-
-
brenda
no activity in Mucor mucedo
-
-
-
brenda
no activity in Mycobacterium phlei
-
-
-
brenda
no activity in Myrothecium roridum
-
-
-
brenda
no activity in Neurospora crassa
-
-
-
brenda
no activity in Oedohysterium insidens
-
-
-
brenda
no activity in Oidiodendron echinulatum
-
-
-
brenda
no activity in Paecilomyces marquandii
-
-
-
brenda
no activity in Penicillium brevicompactum
-
-
-
brenda
no activity in Penicillium patulum
-
-
-
brenda
no activity in Pestalotia viridis
-
-
-
brenda
no activity in Phoma terrestris
-
-
-
brenda
no activity in Phycomyces blakesleeanus
-
-
-
brenda
no activity in Physalospora zeicola
-
-
-
brenda
no activity in Pleospora herbarum
-
-
-
brenda
no activity in Propionibacterium freudenreichii
-
-
-
brenda
no activity in Propionibacterium sp.
-
-
-
brenda
no activity in Proteus inconstans
-
-
-
brenda
no activity in Proteus morganii
-
-
-
brenda
no activity in Pseudomonas aeruginosa
-
-
-
brenda
no activity in Pseudomonas fluorescens
-
-
-
brenda
no activity in Pseudomonas maltophilia
-
-
-
brenda
no activity in Rhizopus nigricans
-
-
-
brenda
no activity in Rhodotorula rubra
-
-
-
brenda
no activity in Saccharomyces fragilis
-
-
-
brenda
no activity in Saccharomyces pastorianus
-
-
-
brenda
no activity in Schizophyllum commune
-
-
-
brenda
no activity in Schizosaccharomyces pombe
-
-
-
brenda
no activity in Scopulariopsis brevicaulis
-
-
-
brenda
no activity in Sepedonium chrysospermum
-
-
-
brenda
no activity in Septoria digitalis
-
-
-
brenda
no activity in Sporonema hiemale
-
-
-
brenda
no activity in Staphylococcus epidermidis
-
-
-
brenda
no activity in Staphylococcus sp.
-
-
-
brenda
no activity in Streptococcus bovis
-
-
-
brenda
no activity in Streptococcus casei
-
-
-
brenda
no activity in Streptococcus faecalis
-
-
-
brenda
no activity in Streptococcus sp.
-
-
-
brenda
no activity in Streptococcus thermophilus
-
-
-
brenda
no activity in Streptomyces sp.
-
-
-
brenda
no activity in Syncephalastrum racemosum
-
-
-
brenda
no activity in Thamnidium elegans
-
-
-
brenda
no activity in Trichothecium roseum
-
-
-
brenda
no activity in Ustilago nigra
-
-
-
brenda
no activity in Verticillium albo-atrum
-
-
-
brenda
no activity in Wardomyces anomalus
-
-
-
brenda
no activity in Yersinia enterocolitica
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
NCIB 8523
-
-
brenda
4 strains generate the enzyme and 2 strains do not
-
-
brenda
ATCC 10778
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
Acetobacter aceti subsp. xylinum
UniProt
brenda
ssp. xylinum
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
gene alsD
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
ATCC 8185
-
-
brenda
strain ATCC 11031
-
-
brenda
-
-
-
brenda
1 strain generates the enzyme and 1 strain does not
-
-
brenda
-
-
-
brenda
strain DSM 2547
-
-
brenda
2 strains generate the enzyme and 3 strains do not
-
-
brenda
5 strains generate the enzyme and 3 strains do not
-
-
brenda
-
-
-
brenda
1 strain generates the enzyme and 1 strain does not
-
-
brenda
-
-
-
brenda
subsp. cremoris
-
-
brenda
subsp. diacetilactis
-
-
brenda
subsp. lactis
-
-
brenda
subsp. lactis biovar diacetylactis
-
-
brenda
subsp. lactis biovar diacetylactis CNRZ 483
-
-
brenda
subsp. lactis, strain NCDO2118
-
-
brenda
-
-
-
brenda
131 strains generate the enzyme and 13 do not
-
-
brenda
38 strain generate the enzyme and 2 strains do not
-
-
brenda
-
-
-
brenda
1 strain generates the enzyme and 1 strain does not
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Sone, H.; Kondo, K.; Fujii, T.; Shimuzu, F.; Tanaka, J.; Inoue, T.
Fermentation properties of brewer's yeast having alpha-acetolactate decarboxylase gene
Proc. Congr. Eur. Brew. Conv.
21
545-552
1987
Klebsiella aerogenes
-
brenda
Rostgaard Jensen, B.; Svendsen, I.; Ottesen, M.
Isolation and characterization of an alpha-acetolactate decarboxylase useful for accelerated beer maturation
Proc. Congr. Eur. Brew. Conv.
21
393-400
1987
Brevibacillus brevis
-
brenda
Goelling, D.; Stahl, U.
Cloning and expression of an alpha-acetolactate decarboxylase gene from Streptococcus lactis subsp. diacetylactis in Escherichia coli
Appl. Environ. Microbiol.
54
1889-1891
1988
Lactococcus lactis, Lactococcus lactis subsp. diacetilactis
brenda
Crout, D.H.G.; Rathbone, D.L.
Biotransformations with acetolactate decarboxylase: unusual conversions of both substrate enantiomers into products of high optical purity
J. Chem. Soc. Chem. Commun.
1988
98-99
1988
Bacillus sp. (in: Bacteria)
-
brenda
Sone, H.; Fujii, T.; Kondo, K.; Shimizu, F.; Tanaka, J.I.; Inoue, T.
Nucleotide sequence and expression of the Enterobacter aerogenes alpha-acetolactate decarboxylase gene in brewer's yeast
Appl. Environ. Microbiol.
54
38-42
1988
Klebsiella aerogenes
brenda
Rasmussen, A.M.; Gibson, R.M.M.; Godtfredsen, S.E.; Ottesen, M.
Purification of alpha-acetolactate decarboxylase from Lactobacillus casei DSM 2547
Carlsberg Res. Commun.
50
73-82
1985
Lacticaseibacillus casei
-
brenda
Crout, D.H.G.; Littlechild, J.; Mitchell, M.B.; Morrey, S.M.
Stereochemistry of the decarboxylation of alpha-acetolactate (2-hydroxy-2-methyl-3-oxobutanoate) by the acetolactate decarboxylase of Klebsiella aerogenes
J. Chem. Soc. Perkin Trans. I
1984
2271-2276
1984
Klebsiella aerogenes
-
brenda
Godtfredsen, S.E.; Rasmussen, A.M.; Ottesen, M.; Rafn, P.; Peitersen, N.
Occurence of alpha-acetolactate decarboxylases among lactic acid bacteria and their utilization for maturation of beer
Appl. Microbiol. Biotechnol.
20
23-28
1984
Lactobacillus acidophilus, Lactiplantibacillus plantarum, Lactobacillus delbrueckii subsp. bulgaricus, Lacticaseibacillus casei, Lactococcus lactis subsp. lactis, Leuconostoc mesenteroides subsp. cremoris, Enterococcus durans, Lactococcus lactis subsp. lactis FD-64-D
-
brenda
Godtfredsen, S.E.; Lorck, H.; Sigsgaard, P.
On the occurrence of alpha-acetolactate decarboxylases among microorganisms
Carlsberg Res. Commun.
48
239-247
1983
Gluconobacter oxydans, Komagataeibacter xylinus, Achromobacter metalcaligenes, Klebsiella aerogenes, Enterobacter cloacae, Aeromonas hydrophila, Aeromonas sp., Brevibacillus brevis, Bacillus cereus, Niallia circulans, Priestia megaterium, Bacillus subtilis, Bacillus licheniformis, Paenibacillus macerans, Paenibacillus polymyxa, Leuconostoc mesenteroides, Brochothrix thermosphacta, Cellulomonas flavigena, Chromobacterium lividum, Rhodococcus equi, Corynebacterium renale, Pantoea agglomerans, Enterobacter sp., Enterococcus faecium, Lactobacillus acidophilus, Lacticaseibacillus casei, Lactobacillus delbrueckii subsp. lactis, Lactococcus lactis subsp. lactis, Fructilactobacillus fructivorans, Lactococcus lactis, Micrococcus luteus, no activity in Acinetobacter sp., no activity in Agrobacterium tumefaciens, no activity in Alcaligenes faecalis, no activity in Ascodesmis nigricans, no activity in Ascoidea rubescens, no activity in Aspergillus clavatus, no activity in Aspergillus niger, no activity in Aureobasidium pullulans, no activity in Bacillus sp., no activity in Botrytis allii, no activity in Brevibacterium divaricatum, no activity in Byssochlamys fulva, no activity in Cephalosporium acremonium, no activity in Cephalosporium spinosum, no activity in Ceratocystis piceae, no activity in Chaetomella terricola, no activity in Chaetomium globosum, no activity in Chromobacterium violaceum, no activity in Chrysosporium keratinophilum, no activity in Citrobacter freundii, no activity in Helminthosporium solani, no activity in Clostridium acetobutyricum, no activity in Clostridium bifermentans, no activity in Clostridium histolyticum, no activity in Clostridium innocuum, no activity in Clostridium perfringens, no activity in Clostridium propionicum, no activity in Clostridium sporogenes, no activity in Coniothyrium carpaticum, no activity in Cunninghamella blakesleeana, no activity in Physalospora zeicola, no activity in Dipodascus aggregatus, no activity in Escherichia coli, no activity in Emericellopsis salmosynnemata, no activity in Epicoccum andropogonis, no activity in Erwinia sp., no activity in Flavobacterium meningosepticum, no activity in Flavobacterium sp., no activity in Fomes annosus, no activity in Acremonium fusioides, no activity in Geotrichum candidum, no activity in Hypomyces solani, no activity in Oedohysterium insidens, no activity in Klebsiella pneumoniae, no activity in Kloeckera apiculata, no activity in Lactobacillus brevis, no activity in Lactobacillus buchneri, no activity in Lactobacillus bulgaricus, no activity in Lactobacillus fermentum, no activity in Lactobacillus helveticus, no activity in Leuconostoc citrovorum, no activity in Melanconium juglandinum, no activity in Micrococcus sp., no activity in Monascus ruber, no activity in Monotospora brevis, no activity in Mucor mucedo, no activity in Mycobacterium phlei, no activity in Myrothecium roridum, no activity in Neurospora crassa, no activity in Oidiodendron echinulatum, no activity in Paecilomyces marquandii, no activity in Penicillium brevicompactum, no activity in Penicillium patulum, no activity in Pestalotia viridis, no activity in Pseudomonas aeruginosa, no activity in Phoma terrestris, no activity in Phycomyces blakesleeanus, no activity in Pleospora herbarum, no activity in Propionibacterium freudenreichii, no activity in Propionibacterium sp., no activity in Proteus inconstans, no activity in Proteus morganii, no activity in Pseudomonas fluorescens, no activity in Pseudomonas maltophilia, no activity in Rhizopus nigricans, no activity in Rhodotorula rubra, no activity in Saccharomyces fragilis, no activity in Saccharomyces pastorianus, no activity in Schizophyllum commune, no activity in Schizosaccharomyces pombe, no activity in Scopulariopsis brevicaulis, no activity in Sepedonium chrysospermum, no activity in Septoria digitalis, no activity in Sporonema hiemale, no activity in Staphylococcus epidermidis, no activity in Staphylococcus sp., no activity in Streptococcus bovis, no activity in Streptococcus casei, no activity in Streptococcus faecalis, no activity in Streptococcus sp., no activity in Streptococcus thermophilus, no activity in Streptomyces sp., no activity in Syncephalastrum racemosum, no activity in Thamnidium elegans, no activity in Trichothecium roseum, no activity in Ustilago nigra, no activity in Verticillium albo-atrum, no activity in Wardomyces anomalus, no activity in Yersinia enterocolitica, Serratia plymuthica, Pseudomonas viridiflava, Serratia marcescens, Streptococcus agalactiae, Streptococcus uberis, Vibrio parahaemolyticus, Lactococcus lactis subsp. cremoris
-
brenda
Cogan, T.M.; O'Dowd, M.; Mellerick, D.
Effects of pH and sugar on acetoin production from citrate by Leuconostoc lactis
Appl. Environ. Microbiol.
41
1-8
1981
Leuconostoc lactis
brenda
Hill, R.K.; Sawada, S.; Arfin, S.M.
Stereochemistry of valine and isoleucine biosynthesis. IV. Synthesis, configuration, and enzymatic specificity of alpha-acetolactate and alpha-aceto-alpha-hydroxybutyrate
Bioorg. Chem.
8
175-189
1979
Acidobacterium aerogenes
-
brenda
Stormer, F.C.
2,3-Butanediol biosynthesis system in Aerobacter aerogenes
Methods Enzymol.
41B
518-533
1975
Klebsiella aerogenes
brenda
Loken, J.P.; Stormer, F.C.
Acetolactate decarboxylase from Aerobacter aerogenes
Eur. J. Biochem.
14
133-137
1970
Klebsiella aerogenes
brenda
Oshiro, T.; Aisaka, K.; Uwajima, T.
Purification and characterization of alpha-acetolactate decarboxylase from Brevibacterium acetylicum
Agric. Biol. Chem.
53
1913-1918
1989
Klebsiella aerogenes, Bacillus licheniformis, Exiguobacterium acetylicum, Lactiplantibacillus plantarum, Micrococcus luteus, Proteus mirabilis, Proteus vulgaris
-
brenda
Goupil-Feuillerat, N.; Cocaign-Bousquet, M.; Godon, J.J.; Ehrlich, S.D.; Renault, P.
Dual role of alpha-acetolactate decarboxylase in Lactococcus lactis subsp. lactis
J. Bacteriol.
179
6285-6293
1997
Bacillus subtilis, Raoultella terrigena, Lactococcus lactis, Oenococcus oeni
brenda
Sone, H.; Fujii, T.; Kondo, K.; Tanaka, J.
Molecular cloning of the gene encoding alpha-acetolactate decarboxylase from Enterobacter aerogenes
J. Biotechnol.
5
87-91
1987
Klebsiella aerogenes
-
brenda
Phalip, V.; Monnet, C.; Schmitt, P.; Renault, P.; Godon, J.J.; Divies, C.
Purification and properties of the alpha-acetolactate decarboxylase from Lactococcus lactis subsp. lactis NCDO 2118
FEBS Lett.
351
95-99
1994
Lactococcus lactis, Lactococcus lactis NCDO 2118
brenda
Fujii, T.; Kondo, K.; Shimizu, F.; Sone, H.; Tanaka, J.I.; Inoue, T.
Application of a ribosomal DNA integration vector in the construction of a brewer's yeast having alpha-acetolactate decarboxylase activity
Appl. Environ. Microbiol.
56
997-1003
1990
Klebsiella aerogenes
brenda
Drake, A.F.; Siligardi, G.; Crout, D.H.G.; Rathbone, D.L.
Applications of vibrational infrared circular dichroism to biological problems: stereochemistry of proton exchange in acetoin (3-hydroxybutan-2-one) catalyzed by acetolactate decarboxylase
J. Chem. Soc. Chem. Commun.
1987
1834-1835
1987
Bacillus sp. (in: Bacteria)
-
brenda
Yamano, S.; Tanaka, J.; Inoue, T.
Cloning and expression of the gene encoding alpha-acetolactate decarboxylase from Acetobacter aceti ssp. xylinum in brewer's yeast
J. Biotechnol.
32
165-171
1994
Acetobacter aceti
brenda
Yamano, S.; Kondo, K.; Tanaka, J.; Inoue, T.
Construction of a brewer's yeast having alpha-acetolactate decarboxylase gene from Acetobacter aceti ssp. xylinum integrated in the genome
J. Biotechnol.
32
173-178
1994
Acetobacter aceti
brenda
Crout, D.H.G.; Lee, E.R.; Rathbone, D.L.
Absolute configuration of the product of the acetolactate synthase reaction by a novel method of analysis using acetolacate decarboxylase
J. Chem. Soc. Perkin Trans. I
1990
1367-1369
1990
Brevibacillus brevis
-
brenda
Najmudin, S.; Andersen, J.T.; Patkar, S.A.; Borchert, T.V.; Crout, D.H.G.; Flp, V.
Purification, crystallization and preliminary X-ray crystallographic studies on acetolactate decarboxylase
Acta Crystallogr. Sect. D
59
1073-1075
2003
Brevibacillus brevis
brenda
Dulieu, C.; Moll, M.; Boudrant, J.; Poncelet, D.
Improved performances and control of beer fermentation using encapsulated alpha-acetolactate decarboxylase and modeling
Biotechnol. Prog.
16
958-965
2000
Saccharomyces cerevisiae
brenda
O'Sullivan, S.M.; Condon, S.; Cogan, T.M.; Sheehan, D.
Purification and characterisation of acetolactate decarboxylase from Leuconostoc lactis NCW1
FEMS Microbiol. Lett.
194
245-249
2001
Leuconostoc lactis, Leuconostoc lactis NCW1
brenda
Goupil-Feuillerat, N.; Corthier, G.; Godon, J.J.; Ehrlich, S.D.; Renault, P.
Transcriptional and translational regulation of alpha-acetolactate decarboxylase of Lactococcus lactis subsp. lactis
J. Bacteriol.
182
5399-5408
2000
Lactococcus lactis
brenda
Aymes, F.; Monnet, C.; Corrieu, G.
Effect of alpha-acetolactate decarboxylase inactivation on alpha-acetolactate and diacetyl production by Lactococcus lactis subsp. lactis biovar diacetylactis
J. Biosci. Bioeng.
87
87-92
1999
Lactococcus lactis
brenda
Monnet, C.; Nardi, M.; Hols, P.; Gulea, M.; Corrieu, G.; Monnet, V.
Regulation of branched-chain amino acid biosynthesis by alpha-acetolactate decarboxylase in Streptococcus thermophilus
Lett. Appl. Microbiol.
36
399-405
2003
Streptococcus thermophilus (Q8L208), Streptococcus thermophilus, Streptococcus thermophilus CNRZ385 (Q8L208), Streptococcus thermophilus CNRZ385
brenda
Curic, M.; de Richelieu, M.; Henriksen, C.M.; Jochumsen, K.V.; Villadsen, J.; Nilsson, D.
Glucose/citrate cometabolism in Lactococcus lactis subsp. lactis biovar diacetylactis with impaired alpha-acetolactate decarboxylase
Metab. Eng.
1
291-298
1999
Lactococcus lactis
brenda
Pedersen, S.; Lange, N.K.; Nissen, A.M.
Novel industrial enzyme applications
Ann. N. Y. Acad. Sci.
750
376-390
1995
Brevibacillus brevis
-
brenda
Fuchs, S.; Pane-Farre, J.; Kohler, C.; Hecker, M.; Engelmann, S.
Anaerobic gene expression in Staphylococcus aureus
J. Bacteriol.
189
4275-4289
2007
Staphylococcus aureus
brenda
Zhao, L.; Bao, Y.; Wang, J.; Liu, B.; An, L.
Optimization and mechanism of diacetyl accumulation by Enterobacter aerogenes mutant UV-3
World J. Microbiol. Biotechnol.
25
57-64
2009
Klebsiella aerogenes, Klebsiella aerogenes 10293
-
brenda
Nielsen, D.R.; Yoon, S.H.; Yuan, C.J.; Prather, K.L.
Metabolic engineering of acetoin and meso-2, 3-butanediol biosynthesis in E. coli
Biotechnol. J.
5
274-284
2010
Lactobacillus delbrueckii subsp. lactis
brenda
Marlow, V.A.; Rea, D.; Najmudin, S.; Wills, M.; Fueloep, V.
Structure and mechanism of acetolactate decarboxylase
ACS Chem. Biol.
8
2339-2344
2013
Bacillus subtilis, Brevibacillus brevis (P23616)
brenda
Zhang, X.; Rao, Z.; Li, J.; Zhou, J.; Yang, T.; Xu, M.; Bao, T.; Zhao, X.
Improving the acidic stability of Staphylococcus aureus alpha-acetolactate decarboxylase in Bacillus subtilis by changing basic residues to acidic residues
Amino Acids
47
707-717
2015
Staphylococcus aureus
brenda
Serebrennikov, V.; Kotova, L.; Glazunov, A.
alpha-Acetolactate overexpression from glucose in the diacetyl producer Lactococcus lactis ssp. lactis bv. diacetylactis B2103, a natural mutant lacking alpha-acetolactate decarboxylase
Appl. Biochem. Microbiol.
50
689-700
2014
Lactococcus lactis, no activity in Lactococcus lactis subsp. lactis bv. diacetylactis strain B2103/74, Lactococcus lactis NRCIM-7590
-
brenda
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
Appl. Microbiol. Biotechnol.
102
6479-6491
2018
Bacillus subtilis, Bacillus subtilis 168
brenda
Shen, X.; Liu, D.; Liu, J.; Wang, Y.; Xu, J.; Yang, Z.; Guo, T.; Niu, H.; Ying, H.
Enhanced production of butanol and acetoin by heterologous expression of an acetolactate decarboxylase in Clostridium acetobutylicum
Biores. Technol.
216
601-606
2016
Bacillus subtilis (Q04777), Bacillus subtilis, Bacillus subtilis 168 (Q04777)
brenda
Cejnar, R.; Hlozkova, K.; Kotrba, P.; Dostalek, P.
Surface-engineered Saccharomyces cerevisiae displaying alpha-acetolactate decarboxylase from Acetobacter aceti ssp xylinum
Biotechnol. Lett.
38
2145-2151
2016
Acetobacter aceti (Q53405), Acetobacter aceti IFO3288/NBRC 3288 (Q53405)
brenda
Guo, Y.; Pan, D.; Ding, H.; Wu, Z.; Sun, Y.; Zeng, X.
Purification and characterization of alpha-acetolactate decarboxylase (ALDC) from newly isolated Lactococcus lactis DX
J. Sci. Food Agric.
95
1655-1661
2015
Lactococcus lactis, Lactococcus lactis DX
brenda
Zhao, C.; Su, H.; Liu, Y.
Catalytic mechanism of acetolactate decarboxylase from Brevibacillus brevis towards both enantiomers of alpha-acetolactate
RSC Adv.
6
80621-80629
2016
Brevibacillus brevis
-
brenda
Zhuang, C.; Zheng, Q.
QM/MM calculations and MD simulations of acetolactate decarboxylase to reveal substrate R/S-acetolactate binding mode and stereoselective catalytic mechansim
RSC Adv.
6
91852-91859
2016
Brevibacillus brevis (P23616)
-
brenda