Information on EC 4.1.1.5 - acetolactate decarboxylase

Word Map on EC 4.1.1.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.1.1.5
-
RECOMMENDED NAME
GeneOntology No.
acetolactate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Butanoate metabolism
-
-
C5-Branched dibasic acid metabolism
-
-
pyruvate fermentation to (R)-acetoin II
-
-
acetoin degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
(2S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase [(3R)-3-hydroxybutan-2-one-forming]
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-02-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ssp. xylinum
-
-
Manually annotated by BRENDA team
Achromobacter metalcaligenes
1 strain generates the enzyme and 2 strains do not
-
-
Manually annotated by BRENDA team
Acidobacterium aerogenes
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
7 strains generate the enzyme and 1 strain does not
-
-
Manually annotated by BRENDA team
8 strains generate the enzyme and 5 strains do not
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ATCC 10778
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 10293
-
-
Manually annotated by BRENDA team
2 strains generate the enzyme and 2 strains does not
-
-
Manually annotated by BRENDA team
3 strains generate the enzyme and 4 strains do not
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
2 strains generate the enzyme and 3 strains do not
-
-
Manually annotated by BRENDA team
one strain generates the enzyme and another strain does not
-
-
Manually annotated by BRENDA team
strain NCDO 2118
-
-
Manually annotated by BRENDA team
subsp. diacetilactis
-
-
Manually annotated by BRENDA team
strain NCW1
-
-
Manually annotated by BRENDA team
2 strains generate the enzyme and 1 strain does not
-
-
Manually annotated by BRENDA team
no activity in Acinetobacter sp.
-
-
-
Manually annotated by BRENDA team
no activity in Agrobacterium tumefaciens
-
-
-
Manually annotated by BRENDA team
no activity in Alcaligenes faecalis
-
-
-
Manually annotated by BRENDA team
no activity in Ascodesmis nigricans
-
-
-
Manually annotated by BRENDA team
no activity in Ascoidea rubescens
-
-
-
Manually annotated by BRENDA team
no activity in Aspergillus clavatus
-
-
-
Manually annotated by BRENDA team
no activity in Aspergillus niger
-
-
-
Manually annotated by BRENDA team
no activity in Aureobasidium pullulans
-
-
-
Manually annotated by BRENDA team
no activity in Bacillus sp.
-
-
-
Manually annotated by BRENDA team
no activity in Botrytis allii
-
-
-
Manually annotated by BRENDA team
no activity in Brevibacterium divaricatum
-
-
-
Manually annotated by BRENDA team
no activity in Byssochlamys fulva
-
-
-
Manually annotated by BRENDA team
no activity in Cephalosporium acremonium
-
-
-
Manually annotated by BRENDA team
no activity in Cephalosporium spinosum
-
-
-
Manually annotated by BRENDA team
no activity in Ceratocystis piceae
-
-
-
Manually annotated by BRENDA team
no activity in Chaetomella terricola
-
-
-
Manually annotated by BRENDA team
no activity in Chaetomium globosum
-
-
-
Manually annotated by BRENDA team
no activity in Chromobacterium violaceum
-
-
-
Manually annotated by BRENDA team
no activity in Chrysosporium keratophilum
-
-
-
Manually annotated by BRENDA team
no activity in Citrobacter bethesda
-
-
-
Manually annotated by BRENDA team
no activity in Cladosporium solani
-
-
-
Manually annotated by BRENDA team
no activity in Clostridium acetobutyricum
-
-
-
Manually annotated by BRENDA team
no activity in Clostridium bifermentans
-
-
-
Manually annotated by BRENDA team
no activity in Clostridium histolyticum
-
-
-
Manually annotated by BRENDA team
no activity in Clostridium innocuum
-
-
-
Manually annotated by BRENDA team
no activity in Clostridium perfringens
-
-
-
Manually annotated by BRENDA team
no activity in Clostridium propionicum
-
-
-
Manually annotated by BRENDA team
no activity in Clostridium sporogenes
-
-
-
Manually annotated by BRENDA team
no activity in Conothyrium carpaticum
-
-
-
Manually annotated by BRENDA team
no activity in Cunninghamella blakesleeana
-
-
-
Manually annotated by BRENDA team
no activity in Dipodascus aggregatus
-
-
-
Manually annotated by BRENDA team
no activity in Emericellopsis salmosynnemata
-
-
-
Manually annotated by BRENDA team
no activity in Epicoccum andropogonis
-
-
-
Manually annotated by BRENDA team
no activity in Erwinia sp.
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
no activity in Flavobacterium meningosepticum
-
-
-
Manually annotated by BRENDA team
no activity in Flavobacterium sp.
-
-
-
Manually annotated by BRENDA team
no activity in Fomes annosus
-
-
-
Manually annotated by BRENDA team
no activity in Fusidium coccineum
-
-
-
Manually annotated by BRENDA team
no activity in Geotrichum candidum
-
-
-
Manually annotated by BRENDA team
no activity in Hypomyces solani
-
-
-
Manually annotated by BRENDA team
no activity in Klebsiella pneumoniae
-
-
-
Manually annotated by BRENDA team
no activity in Kloeckera apiculata
-
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus brevis
-
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus buchneri
-
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus bulgaricus
-
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus fermentum
ATCC 9338
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus helveticus
-
-
-
Manually annotated by BRENDA team
no activity in Leuconostoc citrovorum
-
-
-
Manually annotated by BRENDA team
no activity in Melanconium juglandinum
-
-
-
Manually annotated by BRENDA team
no activity in Micrococcus sp.
-
-
-
Manually annotated by BRENDA team
no activity in Monascus ruber
-
-
-
Manually annotated by BRENDA team
no activity in Monotospora brevis
-
-
-
Manually annotated by BRENDA team
no activity in Mucor mucedo
-
-
-
Manually annotated by BRENDA team
no activity in Mycobacterium phlei
-
-
-
Manually annotated by BRENDA team
no activity in Myrothecium roridum
-
-
-
Manually annotated by BRENDA team
no activity in Neurospora crassa
-
-
-
Manually annotated by BRENDA team
no activity in Oedohysterium insidens
-
-
-
Manually annotated by BRENDA team
no activity in Oidiodendron echinulatum
-
-
-
Manually annotated by BRENDA team
no activity in Paecilomyces marquandii
-
-
-
Manually annotated by BRENDA team
no activity in Penicillium brevicompactum
-
-
-
Manually annotated by BRENDA team
no activity in Penicillium patulum
-
-
-
Manually annotated by BRENDA team
no activity in Pestalotia viridis
-
-
-
Manually annotated by BRENDA team
no activity in Phoma terrestris
-
-
-
Manually annotated by BRENDA team
no activity in Phycomyces blakesleeanus
-
-
-
Manually annotated by BRENDA team
no activity in Physalospora zeicola
-
-
-
Manually annotated by BRENDA team
no activity in Pleospora herbarum
-
-
-
Manually annotated by BRENDA team
no activity in Propionibacterium freudenreichii
-
-
-
Manually annotated by BRENDA team
no activity in Propionibacterium sp.
-
-
-
Manually annotated by BRENDA team
no activity in Proteus inconstans
-
-
-
Manually annotated by BRENDA team
no activity in Proteus morganii
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas aeruginosa
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas fluorescens
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas maltophilia
-
-
-
Manually annotated by BRENDA team
no activity in Rhizopus nigricans
-
-
-
Manually annotated by BRENDA team
no activity in Rhodotorula rubra
-
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces fragilis
-
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces pastorianus
-
-
-
Manually annotated by BRENDA team
no activity in Schizophyllum commune
-
-
-
Manually annotated by BRENDA team
no activity in Schizosaccharomyces pombe
-
-
-
Manually annotated by BRENDA team
no activity in Scopulariopsis brevicaulis
-
-
-
Manually annotated by BRENDA team
no activity in Sepedonium chrysospermum
-
-
-
Manually annotated by BRENDA team
no activity in Septoria digitalis
-
-
-
Manually annotated by BRENDA team
no activity in Sporonema hiemale
-
-
-
Manually annotated by BRENDA team
no activity in Staphylococcus epidermidis
-
-
-
Manually annotated by BRENDA team
no activity in Staphylococcus sp.
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus bovis
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus casei
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus faecalis
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus sp.
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus thermophilus
-
-
-
Manually annotated by BRENDA team
no activity in Streptomyces sp.
-
-
-
Manually annotated by BRENDA team
no activity in Syncephalastrum racemosum
-
-
-
Manually annotated by BRENDA team
no activity in Thamnidium elegans
-
-
-
Manually annotated by BRENDA team
no activity in Trichothecium roseum
-
-
-
Manually annotated by BRENDA team
no activity in Ustilago nigra
-
-
-
Manually annotated by BRENDA team
no activity in Verticillium albo-atrum
-
-
-
Manually annotated by BRENDA team
no activity in Wardomyces anomalus
-
-
-
Manually annotated by BRENDA team
no activity in Yersinia enterocolitica
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
NCIB 8523
-
-
Manually annotated by BRENDA team
4 strains generate the enzyme and 2 strains do not
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain CNRZ385
SwissProt
Manually annotated by BRENDA team
strain CNRZ385
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ALDC does not contain a basic lysine residue capable of forming an imine intermediate prior to decarboxylation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3R)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
show the reaction diagram
transition state analogue acts as substrate and competitive inhibitor
-
-
?
(2R,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
show the reaction diagram
transition state analogue acts as substrate and mixed-type inhibitor
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
show the reaction diagram
(2S,3R)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
show the reaction diagram
transition state analogue acts as substrate and competitive inhibitor
-
-
?
(2S,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
show the reaction diagram
transition state analogue acts as substrate and competitive inhibitor
-
-
?
(2S,3S)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
?
show the reaction diagram
transition state analogue acts as substrate and competitive inhibitor
-
-
?
(R)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
show the reaction diagram
2-Hydroxy-2-ethyl-3-oxobutanoate
3-Hydroxypentan-2-one + CO2
show the reaction diagram
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
show the reaction diagram
2-Hydroxy-2-methyl-3-oxobutanoate
?
show the reaction diagram
alpha-acetolactate + CO2
acetoin
show the reaction diagram
-
-
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
show the reaction diagram
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
show the reaction diagram
2-Hydroxy-2-methyl-3-oxobutanoate
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
-
contains 0.537 nmol of Fe per mg of protein
Zn
-
contains 38.2 nmol of Zn per mg of protein
Zn2+
ALDC is a metalloprotein with a two domain alpha/beta tertiary structure. Three highly conserved histidines 194, 196, and 207 coordinate a Zn2+ ion, together with a conserved glutamate 253 from the C-terminal tail
additional information
-
activity is independent of metals
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R,3R)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
competitive inhibition of the transition state analogue
(2R,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
mixed inhibition of the transition state analogue
(2S,3R)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
competitive inhibition of the transition state analogue
(2S,3S)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
competitive inhibition of the transition state analogue
1,10-phenanthroline
2-phosphoglyceric acid
-
alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together
3-Phosphoglyceric acid
-
alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together
6-phosphogluconic acid
-
alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together
8-Quinolinol
-
-
ADP
-
alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together
ATP
-
alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together
diethyldithiocarbamate
-
-
dihydroxyacetone phosphate
-
alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together
EDTA
-
2 mM Mn2+ restores 82% of the activity, 2 mM Zn2+ restores 69% of the initial activity
fructose 1,6-diphosphate
-
alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together
p-hydroxymercuribenzoate
-
-
phosphoenolpyruvate
-
alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together
Trinitrobenzenesulfonate
-
weak
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
isoleucine
requirement for branched-chain amino acids, control of the pool of alpha-acetolactate by valine, leucine and isoleucine via allosteric activation, valine is more stimulatory than leucine and isoleucine
leucine
valine
requirement for branched-chain amino acids, control of the pool of alpha-acetolactate by valine, leucine and isoleucine via allosteric activation, valine is more stimulatory than leucine and isoleucine
additional information
-
activity is independent of the branched chain amino acids leucine, valine or isoleucine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55
(2R,3R)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
pH 6.0, temperature not specified in the publication
0.78
(2R,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
pH 6.0, temperature not specified in the publication
0.56
(2S,3R)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
pH 6.0, temperature not specified in the publication
0.49
(2S,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
pH 6.0, temperature not specified in the publication
1.3
(S)-2-Hydroxy-2-methyl-3-oxobutanoate
-
pH 6
10
2-hydroxy-2-ethyl-3-oxobutanoate
-
-
0.06 - 75
2-Hydroxy-2-methyl-3-oxobutanoate
additional information
additional information
-
kinetic data
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 66.67
(S)-2-Hydroxy-2-methyl-3-oxobutanoate
5.57
2-Hydroxy-2-methyl-3-oxobutanoate
Lactobacillus casei
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.76
(2R,3R)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
pH 6.0, temperature not specified in the publication
7.68
(2R,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
pH 6.0, temperature not specified in the publication
1.72
(2S,3R)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
pH 6.0, temperature not specified in the publication
0.46
(2S,3S)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+)
pH 6.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.27
culture in the presence of leucine and isoleucine
0.472
culture in the presence of leucine and valine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
-
pH 4.0: about 25% of maximal activity, pH 8.0: about 60% of maximal activity
4 - 7
-
pH 4.0: about 70% of maximal activity, pH 7.0: about 15% of maximal activity
4.7 - 6.5
-
pH 4.7: about 20% of maximal activity, pH 6.5: about 25% of maximal activity
5.4 - 6.9
-
75% of maximal activity at pH 5.4 and at pH 6.9
5.5 - 6.5
-
most active between pH 5.5 and 6.5
5.5 - 7.5
-
pH 5.5: about 60% of maximal activity, pH 7.5: about 70% of maximal activity
5.6 - 7.2
-
pH 5.6: about 60% of maximal activity, pH 7.2: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 50
20 - 50
additional information
-
temperature has a strong effect on the decarboxylation rate of alpha-acetolactate
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3 - 4.4
-
Mono P chromatofocusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
anaerobic growth condition: NADH is regenerated by mixed acid and butanediol fermentation, as indicated by an elevated synthesis level of fermentation enzymes like lactate dehydrogenases (Ldh1 and Ldh2), alcohol dehydrogenases (AdhE and Adh), alpha-acetolactate decarboxylase (BudA1), acetolactate synthase (BudB), and acetoin reductase (SACOL0111) as well as an accumulation of fermentation products as lactate and acetate.
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26500
-
6 * 26500, SDS-PAGE
27500
-
2 * 27500, SDS-PAGE
31000
-
2 * 31000, SDS-PAGE
35000
-
2 * 35000, SDS-PAGE
48000
-
gel filtration
49000
-
2 * 49000, SDS-PAGE
62000
-
gel filtration
70000
-
gel filtration
73000
-
high speed equilibrium centrifugation, disc gel electrophoresis
100000
-
approximately, gel filtration
150000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
additional information
ALDC is a metalloprotein with a two domain alpha/beta tertiary structure. The N-terminal domain comprises a 7-stranded mixed beta-sheet that extends into the equivalent beta-sheet of the 2-fold symmetry-related molecule generating a 14-stranded beta-sheet that spans the physiologically relevant dimeric assembly
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, expressed in Bacillus subtilis JA222, hanging drop vapour-diffusion method, X-ray structure
-
X-ray diffraction crystal structure determination and analysis by single wavelength anomalous dispersion method at 1.1 A resolution, ethane-1,2-diol is used as a cryoprotectant
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
unstable below pH 4 and above pH 9
4643
5 - 8
-
30 min at 37C: complete loss of activity at pH 4, about 60% loss of activity at pH 5, completely stable at pH 7, about 20% loss of activity at pH 8, complete loss of activity at pH 9
4651
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
-
alpha-acetolactate decarboxylase activity decreases as temperatures increases from 20 to 50C
37
-
pH 5, half-life: 15 min. Bovine serum albumin, 1 mg/ml, increases half-life to 4.5 h
40
-
stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Triton X-100 stabilizes
-
very unstable, especially when diluted, at 0.05 mg/ml the activity is totally lost within 24 h at 4C. Addition of bovine serum albumin, 5 mg/ml, allows the preservation of the activity for at least 2 weeks
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, purified, aliquoted ALD, 30% (v/v) glycerol, 3 weeks, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, expressed in Bacillus subtilis JA222
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
aldB gene, gene regulation, organization of the leu-ilv-ald operon
-
aldC gene, expression in Escherichia coli
expressed in Escherichia coli YYC202(DE3) cells
-
expression in Escherichia coli
expression in Saccharomyces carlsbergensis; plasmid pIARL28 is a useful vector for gene transfer into a variety of industrial Saccharomyces strains to meet the requirements of commercial application
-
expression in Saccharomyces cerevisiae
-
expression in Saccharomyces uvarum
-
gene alsD, recombinant expression of wild-type and mutant enzymes
-
overexpression in Bacillus subtilis JA222
-
overexpression in Escherichia coli
-
the gene was integrated in a ribosomal RNA gene of a brewer's yeast by co-transformation with an expression plasmid of G418-resistance gene
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E251A
-
site-directed mutagenesis, the mutant shows highly reduced activity
E251Q
-
site-directed mutagenesis, the mutant shows highly reduced activity
E62A
-
site-directed mutagenesis, the mutant shows highly reduced activity
E62Q
-
site-directed mutagenesis, the mutant shows highly reduced activity
R142A
-
site-directed mutagenesis, the mutant shows highly reduced activity
R142K
-
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
T55A
-
site-directed mutagenesis, the mutant shows 2.5fold increased activity compared to the wild-type enzyme
T55S
-
site-directed mutagenesis, the mutant shows 2fold increased activity compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
synthesis
Show AA Sequence (2637 entries)
Please use the Sequence Search for a specific query.