Information on EC 4.1.1.4 - Acetoacetate decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.1.1.4
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RECOMMENDED NAME
GeneOntology No.
Acetoacetate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetoacetate + H+ = acetone + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetone degradation I (to methylglyoxal)
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acetone degradation III (to propane-1,2-diol)
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isopropanol biosynthesis (engineered)
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ketogenesis
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Metabolic pathways
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Propanoate metabolism
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pyruvate fermentation to acetone
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Synthesis and degradation of ketone bodies
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SYSTEMATIC NAME
IUBMB Comments
acetoacetate carboxy-lyase (acetone-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-03-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain EA 2018
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Manually annotated by BRENDA team
strain AA243, no activity in
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Manually annotated by BRENDA team
ATCC 35319
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Manually annotated by BRENDA team
strain A-57
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-2-Methyl-3-oxobutyrate
Butane-2-one + CO2
show the reaction diagram
-
-
-
-
-
(-)-2-Oxocyclohexanecarboxylate
Cyclohexanone + CO2
show the reaction diagram
-
-
-
-
-
2,4-pentanedione
?
show the reaction diagram
-
-
-
?
2-Oxo-3-phenylpropionic acid
Acetophenone + CO2
show the reaction diagram
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i.e. phenylacetoacetate
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-
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3-oxopentanoate + H+
2-butanone + CO2
show the reaction diagram
Acetoacetate
?
show the reaction diagram
Acetoacetate
Acetone + CO2
show the reaction diagram
acetoacetate + H+
acetone + CO2
show the reaction diagram
acetoacetate + proton
acetone + CO2
show the reaction diagram
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-
-
?
levulinic acid + H+
2-butanone + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
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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
Acetoacetate
?
show the reaction diagram
acetoacetate + H+
acetone + CO2
show the reaction diagram
additional information
?
-
-
acetoacetate decarboxylase from Clostridium acetobutylicum can act as a biocatalyst for decarboxylation of levulinic acid
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Dinitrophenyl acetate
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acetylation and complete inactivation of the enzyme
2,4-Pentanedione
2-oxopropane sulfonate
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Acetic anhydride
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acetylation and complete inactivation of the enzyme
acetonylphosphonate
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competitive, rapidly dissociating
Acetopyruvate
Acetylacetone
Azure B
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slight inhibition at 2-10 mM
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beta-Diketones
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-
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Borohydride
levulinic acid
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substrate inhibition is observed with levulinic acid concentration higher than 5 mM
methylene blue
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complete inhibition at 2 mM
Monovalent anions
p-Chloromercuriphenyl sulfonate
Sodium-2-oxo-propanesulfonate
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competitive
Zn2+
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inhibits at above 5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
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activates about 2fold at 5-10 mM
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acetate
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in pH-controlled cultures, the addition of 20 mM acetate promotes a more vigorous solventogenic fermentation
Butyrate
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in pH-controlled cultures, the addition of 20 mM acetate promotes a more vigorous solventogenic fermentation
methyl viologen
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activates 6.7fold at 10 mM
spo0A
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in gel retardation assays, the C-terminal domains of Spo0A is able to bind fragments of acetoacetate decarboxylase promoter, Spo0A directly controls the shift between acidogenesis and solventogenesis, insertional inactivation of spo0A blocked the formation of solvents
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
3-oxo-3-phenylpropionic acid
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0.94 - 400
acetoacetate
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30 - 1560
acetoacetate
additional information
additional information
Clostridium acetobutylicum
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007
2,4-Pentanedione
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at 25C, in 50 mM phosphate buffer, pH 5.95
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
with levulinic acid
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
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pH 3: about 50% of maximal activity, pH 8: about 40% of maximal activity
3.5 - 8
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activity range, profile overview
5 - 8
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pH 5: about 40% of maximal activity, pH 8: about 25% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
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over 30% of maximal activity at 20C and 45C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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native PAGE
280000
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gel filtration
340000
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meniscus depletion method
365000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodecamer
homododecamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AAD complexed with 2,4-pentanedione, hanging drop vapor diffusion method, using 18-20% (v/v) glycerol, 40 mM phosphate buffer, pH 5.95, 100 mM sarcosine and 14-15% (w/v) PEG 3350
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AAD complexed with 2,4-pentanedione, hanging drop vapor diffusion method, using 18-20% (v/v) glycerol, 40 mM phosphate buffer, pH 5.95, 100 mM sarcosine and 14-15% (w/v) PEG 3350
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
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or lower, rapid and irreversible denaturation
4530
4 - 9
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25C, stable
4527
5 - 9
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stable
4530
5.5 - 9
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4C, 23 h, stable
4523
10
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or higher, rapid and irreversible denaturation
4530
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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pH 4-9, stable
60
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30 min, stable up to
70
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above, biphasic irreversible inactivation
85
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30 min: 86% loss of activity, without addition of acetylacetone, stable in presence of 10 mM acetylacetone
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rather easily inactivated by urea, guanidinium chloride and SDS
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the enzyme dissociates into subunit dimers at pH 8 in 4 M urea solution at low temperature. The subunit dimers can be reassociated to form native, active enzyme by diluting the urea solution with phosphate buffer at pH 6.0 in the presence of dithiothreitol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and S-200 gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain JM109
expressed in Escherichia coli strains ATCC 11303 and TA11
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expression in Escherichia coli
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gene aadc encoded in the sol operon, cloning of gene fragments aadc358-1 and aadc358-2 in Escherichia coli strain DH5alpha, expression as GFP-tagged enzyme
gene aadc, cloning in Escherichia coli strain DH5alpha, expression as GFP-tagged enzyme
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), best induction over 24 h at 20C with 1 mM IPTG
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E61Q
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the catalytic activity of the mutant shows a decrease in kcat (about 20fold with no change in Km)
R29Q
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the catalytic activity of Arg29Gln does not increase at pH values above the wild type optimum for AAD of about 5.4
E61Q
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the catalytic activity of the mutant shows a decrease in kcat (about 20fold with no change in Km)
K115C
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mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities
K115Q
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mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities
R29Q
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the catalytic activity of Arg29Gln does not increase at pH values above the wild type optimum for AAD of about 5.4
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
synthesis
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acetoacetate decarboxylase from Clostridium acetobutylicum can act as a biocatalyst for decarboxylation of levulinic acid in an enzymatic system for synthesis of 2-butanone from levulinic acid
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