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J Bacteriol, February 1998, p. 667-673, Vol. 180, No. 3
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Expression and Characterization of (R)-Specific Enoyl Coenzyme A Hydratase Involved in Polyhydroxyalkanoate Biosynthesis by Aeromonas caviae

Toshiaki Fukui,1 Naofumi Shiomi,2 and Yoshiharu Doi1,*

Polymer Chemistry Laboratory, The Institute of Physical and Chemical Research (RIKEN), Hirosawa 2-1, Wako-shi, Saitama 351-01,1 and Department of Human Sciences, Kobe College, Okadayama 4-1, Nishinomiya-shi, Hyogo 662,2 Japan

Received 13 August 1997/Accepted 25 November 1997

Complementation analysis of a polyhydroxyalkanoate (PHA)-negative mutant of Aeromonas caviae proved that ORF3 in the pha locus (a 402-bp gene located downstream of the PHA synthase gene) participates in PHA biosynthesis on alkanoic acids, and the ORF3 gene is here referred to as phaJAc. Escherichia coli BL21(DE3) carrying phaJAc under the control of the T7 promoter overexpressed enoyl coenzyme A (enoyl-CoA) hydratase, which was purified by one-step anion-exchange chromatography. The N-terminal amino acid sequence of the purified hydratase corresponded to the amino acid sequence deduced from the nucleotide sequence of phaJAc except for the initial Met residue. The enoyl-CoA hydratase encoded by phaJAc exhibited (R)-specific hydration activity toward trans-2-enoyl-CoA with four to six carbon atoms. These results have demonstrated that (R)-specific hydration of 2-enoyl-CoA catalyzed by the translated product of phaJAc is a channeling pathway for supplying (R)-3-hydroxyacyl-CoA monomer units from fatty acid beta -oxidation to poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biosynthesis in A. caviae.

* Corresponding author. Mailing address: Polymer Chemistry Laboratory, The Institute of Physical and Chemical Research (RIKEN), Hirosawa 2-1, Wako-shi, Saitama 351-01, Japan. Phone: 81-48-467-9402. Fax: 81-48-462-4667. E-mail: ydoi{at}postman.riken.go.jp.




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