6.4.1.6: acetone carboxylase
This is an abbreviated version!
For detailed information about acetone carboxylase, go to the full flat file.
Word Map on EC 6.4.1.6
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6.4.1.6
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acetoacetate
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xanthobacter
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rhodobacter
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capsulatus
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carboxylases
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autotrophicus
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denitrify
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butanone
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acetophenone
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acetone-grown
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alpha2beta2gamma2
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isopropanol
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phototrophic
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heterohexameric
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alicycliphilus
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rhodomicrobium
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aromatoleum
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thiolysis
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ethylbenzene
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vannielii
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benzoylacetate
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thiosphaera
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nitrate-dependent
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nitrate-reducing
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pantotropha
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aromaticum
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acetoacetyl-coa
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alkenes
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metallidurans
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cupriavidus
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medicine
- 6.4.1.6
- acetoacetate
- xanthobacter
-
rhodobacter
- capsulatus
- carboxylases
- autotrophicus
-
denitrify
- butanone
- acetophenone
-
acetone-grown
-
alpha2beta2gamma2
- isopropanol
-
phototrophic
-
heterohexameric
- alicycliphilus
-
rhodomicrobium
-
aromatoleum
-
thiolysis
- ethylbenzene
- vannielii
-
benzoylacetate
-
thiosphaera
-
nitrate-dependent
-
nitrate-reducing
- pantotropha
- aromaticum
- acetoacetyl-coa
- alkenes
- metallidurans
-
cupriavidus
- medicine
Reaction
Synonyms
acetone carboxylase, acetone-carboxylating enzyme, ACX, AcxA, AcxB, AcxC, Alide_1502, Alide_1503, Alide_1504, carboxylase, acetone
ECTree
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Metals Ions
Metals Ions on EC 6.4.1.6 - acetone carboxylase
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K+
Mg2+
Mn2+
NH4+
additional information
K+
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monovalent ion, K+ or NH4+, at concentration of 20-80 mM, required for optimal acetone carboxylase activity
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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
Mn2+
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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
NH4+
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monovalent ion, K+ or NH4+, at concentration of 20-80 mM, required for optimal acetone carboxylase activity
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dependent on the presence of a divalent metal
additional information
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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