Affiliation:
1. Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwake, Sakyo-ku, Kyoto 606-8502, Japan
Abstract
ABSTRACT
In the propane-utilizing bacterium
Gordonia
sp. strain TY-5, propane was shown to be oxidized to 2-propanol and then further oxidized to acetone. In this study, the subsequent metabolism of acetone was studied. Acetone-induced proteins were found in extracts of cells induced by acetone, and a gene cluster designated
acmAB
was cloned on the basis of the N-terminal amino acid sequences of acetone-induced proteins. The
acmA
and
acmB
genes encode a Baeyer-Villiger monooxygenase (BVMO) and esterase, respectively. The BVMO encoded by
acmA
was purified from acetone-induced cells of
Gordonia
sp. strain TY-5 and characterized. The BVMO exhibited NADPH-dependent oxidation activity for linear ketones (C
3
to C
10
) and cyclic ketones (C
4
to C
8
).
Escherichia coli
expressing the
acmA
gene oxidized acetone to methyl acetate, and
E. coli
expressing the
acmB
gene hydrolyzed methyl acetate. Northern blot analyses revealed that polycistronic transcription of the
acmAB
gene cluster was induced by propane, 2-propanol, and acetone. These results indicate that the
acmAB
gene products play an important role in the metabolism of acetone derived from propane oxidation and clarify the propane metabolism pathway of strain TY-5 (propane → 2-propanol → acetone → methyl acetate → acetic acid + methanol). This paper provides the first evidence for BVMO-dependent acetone metabolism.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
96 articles.
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