Purification and characterization of the acetone carboxylase of Cupriavidus metallidurans strain CH34.

Butanones; Protein Subunits; Acetone; methylethyl ketone; Carboxy-Lyases; acetone carboxylase; 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; Substrate Specificity; Temperature; 2-butanone; Genome analysis; Key enzymes; Biotechnology; Food Science; Applied Microbiology and Biotechnology; Ecology

Abstract :

[en] 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.

Disciplines :

Zoology

Author, co-author :

Rosier, Caroline ; Université de Mons - UMONS > Faculté des Sciences > Protéomie et Microbiologie

Leys, Natalie; Expert Group for Molecular and Cellular Biology, Mol, Belgium

Henoumont, Céline ; Department of General, Organic and Biomedical Chemistry, NMR and Molecular Imaging Laboratory, Mons, Belgium

Mergeay, Maximilien ; Université de Mons - UMONS > Faculté des Sciences > Protéomie et Microbiologie ; Expert Group for Molecular and Cellular Biology, Mol, Belgium

Wattiez, Ruddy ; Université de Mons - UMONS > Faculté des Sciences > Service de Protéomie et Microbiologie

Language :

English

Title :

Purification and characterization of the acetone carboxylase of Cupriavidus metallidurans strain CH34.

Publication date :

June 2012

Journal title :

Applied and Environmental Microbiology

ISSN :

0099-2240

eISSN :

1098-5336

Publisher :

American Society for Microbiology, United States

Volume :

Issue :

Pages :

4516 - 4518

Peer reviewed :

Peer Reviewed verified by ORBi

Additional URL :

https://journals.asm.org/doi/pdf/10.1128/AEM.07974-11

Research unit :

S828 - Protéomie et Microbiologie

Research institute :

R100 - Institut des Biosciences

Available on ORBi UMONS :

since 03 April 2024

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Bibliography

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