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PMID:22492439

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Citation

Rosier, C, Leys, N, Henoumont, C, Mergeay, M and Wattiez, R (2012) Purification and characterization of the acetone carboxylase of Cupriavidus metallidurans strain CH34. Appl. Environ. Microbiol. 78:4516-8

Abstract

Acetone carboxylase (Acx) is a key enzyme involved in the biodegradation of acetone by bacteria. Except for the Helicobacteraceae family, genome analyses revealed that bacteria that possess an Acx, such as Cupriavidus metallidurans strain CH34, are associated with soil. The Acx of CH34 forms the heterohexameric complex α(2)β(2)γ(2) and can carboxylate only acetone and 2-butanone in an ATP-dependent reaction to acetoacetate and 3-keto-2-methylbutyrate, respectively.

Links

PubMed PMC3370517 Online version:10.1128/AEM.07974-11

Keywords

Acetone/metabolism; Butanones/metabolism; Carboxy-Lyases/chemistry; Carboxy-Lyases/isolation & purification; Carboxy-Lyases/metabolism; Cupriavidus/enzymology; Electrophoresis, Polyacrylamide Gel; Enzyme Stability; Hydrogen-Ion Concentration; Protein Multimerization; Protein Subunits; Substrate Specificity; Temperature

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

RALME:Q1LFV2

GO:0018710: acetone carboxylase activity

ECO:0000314:

F

Figure 3.

complete
CACAO 8145

RALME:Q1LFV4

GO:0018710: acetone carboxylase activity

ECO:0000314:

F

Figure 3.

complete
CACAO 8146

RALME:Q1LFV3

GO:0018710: acetone carboxylase activity

ECO:0000314:

F

Figure 3.

complete
CACAO 8147


See also

References

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