Requires Mg2+ and ATP. The reaction involves separate phosphorylation of hydrogencarbonate and acetone, forming carboxyphosphate and phosphoenolacetone, respectively, which are combined to form the final product. The enzyme from Xanthobacter sp. strain Py2 also carboxylates butan-2-one to 3-oxopentanoate.
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SYSTEMATIC NAME
IUBMB Comments
acetone:carbon-dioxide ligase (AMP-forming)
Requires Mg2+ and ATP. The reaction involves separate phosphorylation of hydrogencarbonate and acetone, forming carboxyphosphate and phosphoenolacetone, respectively, which are combined to form the final product. The enzyme from Xanthobacter sp. strain Py2 also carboxylates butan-2-one to 3-oxopentanoate.
it is proposed that alpha-abstraction from acetone occurs in concert with transfer of the gamma-phosphoryl group of ATP to the carbonyl oxygen, generating phosphoenol acetone as the activated nucleophile for attack on CO2
it is proposed that alpha-abstraction from acetone occurs in concert with transfer of the gamma-phosphoryl group of ATP to the carbonyl oxygen, generating phosphoenol acetone as the activated nucleophile for attack on CO2
2-pentanone, 3-pentanone and 2-hexanone as well as short-chain aliphatic alkanes and alkenes, including propane, are substrates. Several other nucleoside triphosphates are used
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
addition of Fe2+, Mn2+, Zn2+, Ca2+, Co2+, Cu2+ or Ni2+ do not stimulate the enzyme activity above the maximal levels obtained in the presence of Mg2+ alone
nitrate-dependent acetone degradation is activated by carboxylation of acetone and follows a proposed acetone degradation pathway, using an acetone carboxylase converting acetone to acetoacetate, an AMP-dependent synthetase/ligase converting acetoacetate to acetoacetyl-CoA, and an acetyl-CoA acetyltransferase cleaving acetoacetyl-CoA to two acetyl-CoA
nitrate-dependent acetone degradation is activated by carboxylation of acetone and follows a proposed acetone degradation pathway, using an acetone carboxylase converting acetone to acetoacetate, an AMP-dependent synthetase/ligase converting acetoacetate to acetoacetyl-CoA, and an acetyl-CoA acetyltransferase cleaving acetoacetyl-CoA to two acetyl-CoA
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
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
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
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
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
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
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
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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
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
DEAE-Sepharose chromatography, but hydrophobic interaction, gel filtration and anion-exchange chromatography by Q-Sepharose resulted in large loss of activity
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
Assay and properties of acetone carboxylase, a novel enzyme involved in acetone-dependent growth and CO2 fixation in Rhodobacter capsulatus and other photosynthetic and denitrifying bacteria
Biochemical, molecular, and genetic analyses of the acetone carboxylases from Xanthobacter autotrophicus strain Py2 and Rhodobacter capsulatus strain B10
Oosterkamp, M.; Boeren, S.; Atashgahi, S.; Plugge, C.; Schaap, P.; Stams, A.
Proteomic analysis of nitrate-dependent acetone degradation by Alicycliphilus denitrificans strain BC
FEMS Microbiol. Lett.
362
fnv080
2015
Alicycliphilus denitrificans (A0A858ZRU9 and A0A858ZS51 and A0A858ZRP5), Alicycliphilus denitrificans BC (A0A858ZRU9 and A0A858ZS51 and A0A858ZRP5), Alicycliphilus denitrificans BC