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Information on EC 4.1.1.5 - acetolactate decarboxylase and Organism(s) Bacillus subtilis and UniProt Accession Q04777

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.5 acetolactate decarboxylase
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Bacillus subtilis
UNIPROT: Q04777 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
alpha-acetolactate decarboxylase, acetolactate decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-Acetolactate decarboxylase
-
alpha-Acetolactate decarboxylase
-
-
-
-
Decarboxylase, acetolactate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
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
-
-
-
?
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
show the reaction diagram
-
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
show the reaction diagram
2-Hydroxy-2-methyl-3-oxobutanoate
(R)-3-Hydroxybutan-2-one + CO2
show the reaction diagram
DL-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme isomerizes (S)-2-acetohydroxybutyrate to (R)-3-hydroxypentan-2-one
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
-
-
?
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
show the reaction diagram
-
-
-
-
?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
(3R)-3-hydroxybutan-2-one + CO2
show the reaction diagram
additional information
?
-
-
the enzyme isomerizes (S)-2-acetohydroxybutyrate to (R)-3-hydroxypentan-2-one
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
about 110% activity at 1 mM
Ca2+
-
about 160% activity at 1 mM
Mg2+
-
about 120% activity at 1 mM
Zn2+
-
the enzyme contains a zinc ion and shows about 130% activity at 1 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
about 20% residual activity at 1 mM
Fe2+
-
about 60% residual activity at 1 mM
Mn2+
-
about 70% residual activity at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21
DL-2-hydroxy-2-methyl-3-oxobutanoate
-
at pH 6.0 and 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2
DL-2-hydroxy-2-methyl-3-oxobutanoate
-
at pH 6.0 and 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
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
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site-directed mutagenesis, the mutant shows highly reduced activity
E62Q
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site-directed mutagenesis, the mutant shows highly reduced activity
R142A
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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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.5
-
the enzyme activityremains stable between pH 4.5 and 8.5
746865
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap DEAE column chromatography and Superdex 200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Clostridium acetobutylicum strain B3
expressed in Escherichia coli BL21(DE3) cells
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gene alsD, recombinant expression of wild-type and mutant enzymes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Godtfredsen, S.E.; Lorck, H.; Sigsgaard, P.
On the occurrence of alpha-acetolactate decarboxylases among microorganisms
Carlsberg Res. Commun.
48
239-247
1983
Achromobacter metalcaligenes, Aeromonas hydrophila, Aeromonas sp., Bacillus cereus, Bacillus licheniformis, Bacillus subtilis, Brevibacillus brevis, Brochothrix thermosphacta, Cellulomonas flavigena, Chromobacterium lividum, Corynebacterium renale, Enterobacter cloacae, Enterobacter sp., Enterococcus faecium, Fructilactobacillus fructivorans, Gluconobacter oxydans, Klebsiella aerogenes, Komagataeibacter xylinus, Lacticaseibacillus casei, Lactobacillus acidophilus, Lactobacillus delbrueckii subsp. lactis, Lactococcus lactis, Lactococcus lactis subsp. lactis, Leuconostoc mesenteroides, Micrococcus luteus, Niallia circulans, 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 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 Helminthosporium solani, Paenibacillus macerans, Paenibacillus polymyxa, Pantoea agglomerans, Priestia megaterium, Rhodococcus equi, no activity in Acremonium fusioides, no activity in Dipodascus aggregatus, no activity in Emericellopsis salmosynnemata, no activity in Epicoccum andropogonis, no activity in Erwinia sp., no activity in Escherichia coli, no activity in Flavobacterium meningosepticum, no activity in Flavobacterium sp., no activity in Fomes annosus, no activity in Geotrichum candidum, no activity in Hypomyces solani, 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 Oedohysterium insidens, 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 Phoma terrestris, no activity in Phycomyces blakesleeanus, no activity in Physalospora zeicola, 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 aeruginosa, 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, Lactococcus lactis subsp. cremoris, 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, Pseudomonas viridiflava, Serratia marcescens, Serratia plymuthica, Streptococcus agalactiae, Streptococcus uberis, Vibrio parahaemolyticus
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Manually annotated by BRENDA team
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, Lactococcus lactis, Oenococcus oeni, Raoultella terrigena
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team