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

Caroline Rosier; Natalie Leys; Céline Henoumont; Max Mergeay; Ruddy Wattiez; Rob Van Houdt

doi:10.1128/AEM.07974-11

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

Caroline Rosier, Natalie Leys, Céline Henoumont, Max Mergeay, Ruddy Wattiez, Rob Van Houdt

Research output › peer-review

Abstract

Acetone carboxylase (Acx) is a key enzyme involved in the biodegradation of acetone by bacteria. Except for the Helicobacteriaceae family, genome analyses revealed that bacterial that possess Acx are associated to the soil such as Cupriavidus metallidurans strain CH34. Acx of CH34 forms a heterohexameric complex α2β2γ2 and can only carboxylate acetone and 2-butanone in an ATP-dependent reaction to acetoacetate and 3-keto-2-methylbutyrate, respectively.

Original language	English
Pages (from-to)	4516-4518
Journal	Applied and Environmental Microbiology
Volume	78
Issue number	12
DOIs	https://doi.org/10.1128/AEM.07974-11
State	Published - Jun 2012

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title = "Purification and characterization of the acetone carboxylase of Cupriavidus metallidurans strain CH34",

abstract = "Acetone carboxylase (Acx) is a key enzyme involved in the biodegradation of acetone by bacteria. Except for the Helicobacteriaceae family, genome analyses revealed that bacterial that possess Acx are associated to the soil such as Cupriavidus metallidurans strain CH34. Acx of CH34 forms a heterohexameric complex α2β2γ2 and can only carboxylate acetone and 2-butanone in an ATP-dependent reaction to acetoacetate and 3-keto-2-methylbutyrate, respectively.",

keywords = "Acetone carboxylase, acetone metabolism, Cupriavidus metallidurans CH34",

author = "Caroline Rosier and Natalie Leys and C{\'e}line Henoumont and Max Mergeay and Ruddy Wattiez and {Van Houdt}, Rob",

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T1 - Purification and characterization of the acetone carboxylase of Cupriavidus metallidurans strain CH34

AU - Rosier, Caroline

AU - Leys, Natalie

AU - Henoumont, Céline

AU - Mergeay, Max

AU - Wattiez, Ruddy

A2 - Van Houdt, Rob

N1 - Score = 10

PY - 2012/6

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N2 - Acetone carboxylase (Acx) is a key enzyme involved in the biodegradation of acetone by bacteria. Except for the Helicobacteriaceae family, genome analyses revealed that bacterial that possess Acx are associated to the soil such as Cupriavidus metallidurans strain CH34. Acx of CH34 forms a heterohexameric complex α2β2γ2 and can only carboxylate acetone and 2-butanone in an ATP-dependent reaction to acetoacetate and 3-keto-2-methylbutyrate, respectively.

AB - Acetone carboxylase (Acx) is a key enzyme involved in the biodegradation of acetone by bacteria. Except for the Helicobacteriaceae family, genome analyses revealed that bacterial that possess Acx are associated to the soil such as Cupriavidus metallidurans strain CH34. Acx of CH34 forms a heterohexameric complex α2β2γ2 and can only carboxylate acetone and 2-butanone in an ATP-dependent reaction to acetoacetate and 3-keto-2-methylbutyrate, respectively.

KW - Acetone carboxylase

KW - acetone metabolism

KW - Cupriavidus metallidurans CH34

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UR - http://knowledgecentre.sckcen.be/so2/bibref/9710

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VL - 78

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JO - Applied and Environmental Microbiology

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