Information on EC 6.4.1.6 - acetone carboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.4.1.6
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RECOMMENDED NAME
GeneOntology No.
acetone carboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetone + CO2 + ATP + 2 H2O = acetoacetate + AMP + 2 phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetone degradation II (to acetoacetate)
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propanol degradation
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SYSTEMATIC NAME
IUBMB Comments
acetone:carbon-dioxide ligase (AMP-forming)
Requires Mg2+ and ATP. The enzyme from Xanthobacter sp. strain Py2 also carboxylates butan-2-one to 3-oxopentanoate.
CAS REGISTRY NUMBER
COMMENTARY hide
189258-15-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from strain KN Bun08 and K601T
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Manually annotated by BRENDA team
strain CH34
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Manually annotated by BRENDA team
LMD82.1
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Manually annotated by BRENDA team
strain B10
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Manually annotated by BRENDA team
B276, ATCC 31338, formerly Nocardia corallina
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Manually annotated by BRENDA team
strain Py2
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-butanone + CO2 + ATP + H2O
2-methyl-3-oxobutanoate + AMP + phosphate
show the reaction diagram
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-
-
-
?
acetone + CO2 + ATP + H2O
acetoacetate + AMP + phosphate
show the reaction diagram
acetone + CO2 + GTP + H2O
acetoacetate + GMP + phosphate
show the reaction diagram
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better activity than with ATP
-
?
butanone + CO2 + ATP + H2O
3-oxopentanoate + AMP + phosphate
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
acetone + CO2 + ATP + H2O
acetoacetate + AMP + phosphate
show the reaction diagram
butanone + CO2 + ATP + H2O
3-oxopentanoate + AMP + phosphate
show the reaction diagram
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strain KN Bun08 also carboxylates also butanone
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-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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nucleoside triphosphate required, ATP does not support acetone carboxylation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
-
contains 0.7 mol Fe per mol of enzyme
KHCO3
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stimulate the acetone carboxylase activity
Mn
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contains 1.3 mol Mn per mol of enzyme
Mn2+
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enzyme contains 1.9 Mn2+ per alpha2beta2gamma2 multimer, tightly bound and not removed upon dialysis against various metal ion chelators. Presence of a mononuclear Mn2+ center with possible spin coupling of two mononuclear sites. Manganese is essential for acetone carboxylation; tightly bound to the enzyme and not removed upon dialysis against various metal chelators. Presence of a mononuclear Mn2+ center, with possible spin coupling of two mononuclear sites. Mn2+ is essential for acetone carboxylation
Rb+
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monovalent cation required: K+, Rb+ or NH4+
Zn
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contains 1.0 mol Zn per mol of enzyme
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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in high concentrations
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
CoA
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stimulates acetone-dependent CO2 fixation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0078 - 0.03
acetone
0.122
ATP
0.0000042 - 4.17
CO2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.33
acetone
Xanthobacter autotrophicus
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0015 - 0.003
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cell extracts
0.014
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with ITP as nucleoside triphosphate
0.016
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with GTP as nucleoside triphosphate
0.07 - 0.15
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cell suspension
0.094
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usage of butanone
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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not present at detectable levels in cells grown with carbon sources other than acetone
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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1 * 85000, 1 * 74000, 1 * 16000, SDS-PAGE
19000
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SDS-PAGE, alpha subunit
68000
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alpha2beta2gamma2, 2 * 79000 + 2 * 68000 + 2 * 23000, SDS-PAGE
68400
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1 * 68400, 1 * 78800, 1 * 23000 by SDS-PAGE and 1 * 78300, 1 * 85300, 1 * 19600 by mass spectrometry. Subunits have an alpha2beta2gamma2 quaternary structure
70000
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x * 70000 + x * 85000, also 60000 Da and small amounts of 35000 Da subunits exist, SDS-PAGE
74000
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1 * 85000, 1 * 74000, 1 * 16000, SDS-PAGE
76000
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SDS-PAGE, alpha subunit
78800
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1 * 68400, 1 * 78800, 1 * 23000 by SDS-PAGE and 1 * 78300, 1 * 85300, 1 * 19600 by mass spectrometry. Subunits have an alpha2beta2gamma2 quaternary structure
79000
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alpha2beta2gamma2, 2 * 79000 + 2 * 68000 + 2 * 23000, SDS-PAGE
86000
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SDS-PAGE, alpha subunit
353000
388000
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gel filtration
additional information
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three bands observed with SDS-PAGE: 85000, 78000, 20000 Da
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. The enzyme crystallizes in a primitive orthorhombic point group P222, with unit-cell parameters a = 76.2 A, b = 122.0 A, c = 264.2 A. One alphabetagamma half of the large protein complex is located in the asymmetric unit in this crystal form, 3.2 A resolution
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, enzyme in cell extract, stable for several days
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to oxygen
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662000
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 6.5-8.0, activity stable for several days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose chromatography, but hydrophobic interaction, gel filtration and anion-exchange chromatography by Q-Sepharose resulted in large loss of activity
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DEAE-Sepharose chromatography, gel filtration with Sephacryl S-300 column, HiLoad Q-Sepharose column
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enriched from cell extracts of Alicycliphilus denitrificans by two subsequent DEAE Sepharose column procedures
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ion-exchange chromatography
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using anion DEAE-Sepharose chromatography followed by Sephacryl S300 molecular filtration
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the AcxA, AcxB and AcxC subunit proteins are expressed at higher levels in the sensor kinase arsS mutant strains than in the wild type strains
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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inactivation of operon acxABC encoding acetone carboxylase with a chloramphenicol resistance cassette. In mouse colonization studies the numbers of Helicobacter pylori recovered from mice inoculated with the acxB:cat mutant are generally one to two orders of magnitude lower than those recovered from mice inoculated with the parental strain
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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inactivation of operon acxABC encoding acetone carboxylase with a chloramphenicol resistance cassette. In mouse colonization studies the numbers of Helicobacter pylori recovered from mice inoculated with the acxB:cat mutant are generally one to two orders of magnitude lower than those recovered from mice inoculated with the parental strain
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