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J Bacteriol, February 1998, p. 667-673, Vol. 180, No. 3
Polymer Chemistry Laboratory,
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
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
-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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