Abstract
The tetrachloroethene (PCE) reductive dehalogenase (encoded by the pceA gene and designated PceA dehalogenase) of Desulfitobacterium sp. strain Y51 was purified and characterized. The expression of the enzyme was highly induced in the presence of PCE and trichloroethene (TCE). The purified enzyme catalyzed the reductive dehalogenation of PCE via TCE to cis-1,2-dichloroethene at a specific activity of 113.6 nmol x min(-1) x mg of protein(-1). The apparent K(m) values for PCE and TCE were 105.7 and 535.3 microM, respectively. Chlorinated ethenes other than PCE and TCE were not dehalogenated. However, the enzyme exhibited dehalogenation activity for various chlorinated ethanes such as hexachloroethane, pentachloroethane, 1,1,1,2-tetrachloroethane, and 1,1,2,2-tetrachloroethane. The pceA gene of Desulfitobacterium sp. strain Y51 was identified in a 2.8-kb DNA fragment and used to express the protein in Escherichia coli for the preparation of antibodies. Immunoblot analyses located PceA in the periplasm of the cell.
MeSH Terms
Amino Acid Sequence
Cloning, Molecular
Cross Reactions
Electrophoresis, Polyacrylamide Gel
Enzyme Activation
Escherichia coli/genetics
Gram-Positive Bacteria/enzymology,genetics
Molecular Sequence Data
Oxidoreductases/genetics,immunology,metabolism
Sequence Analysis
Sequence Homology, Amino Acid
Chemicals
Oxidoreductases
tetrachloroethene dehalogenase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Suyama Akiko
Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka 812-8581. Towakagaku Co., Ltd., Hiroshima 730-0841, Japan.
Yamashita Masaki
Yoshino Sadazo
Furukawa Kensuke
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