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

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Purification and characterization of the acetone carboxylase of Cupriavidus metallidurans strain CH34. / Rosier, Caroline; Leys, Natalie; Henoumont, Céline; Mergeay, Max; Wattiez, Ruddy; Van Houdt, Rob (Peer reviewer).

In: Applied and Environmental Microbiology, Vol. 78, No. 12, 06.2012, p. 4516-4518.

Research output: Contribution to journalArticle

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Rosier, C, Leys, N, Henoumont, C, Mergeay, M, Wattiez, R & Van Houdt, R 2012, 'Purification and characterization of the acetone carboxylase of Cupriavidus metallidurans strain CH34', Applied and Environmental Microbiology, vol. 78, no. 12, pp. 4516-4518. https://doi.org/10.1128/AEM.07974-11

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Rosier, Caroline ; Leys, Natalie ; Henoumont, Céline ; Mergeay, Max ; Wattiez, Ruddy ; Van Houdt, Rob. / Purification and characterization of the acetone carboxylase of Cupriavidus metallidurans strain CH34. In: Applied and Environmental Microbiology. 2012 ; Vol. 78, No. 12. pp. 4516-4518.

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@article{49789e179c6d47c093250074dc0bf44c,
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",
note = "Score = 10",
year = "2012",
month = "6",
doi = "10.1128/AEM.07974-11",
language = "English",
volume = "78",
pages = "4516--4518",
journal = "Applied and Environmental Microbiology",
issn = "0099-2240",
publisher = "ASMsociety - American Society for Microbiology",
number = "12",

}

RIS - Download

TY - JOUR

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

Y1 - 2012/6

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

UR - http://ecm.sckcen.be/OTCS/llisapi.dll/open/ezp_125811

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

U2 - 10.1128/AEM.07974-11

DO - 10.1128/AEM.07974-11

M3 - Article

VL - 78

SP - 4516

EP - 4518

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

SN - 0099-2240

IS - 12

ER -

ID: 113000