Characterization of tetrachlorohydroquinone reductive dehalogenase from Sphingomonas sp. UG30

Tetrachlorohydroquinone reductive dehalogenase (PcpC) is the second of three enzymes that catalyze the initial degradation of pentachlorophenol in Sphingomonas sp. UG30 and several other bacterial strains. The UG30 PcpC shares a high degree (94%) of primary sequence identity with the well-studied Pc...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2002-12, Vol.299 (4), p.634-640
Main Authors: Habash, M.B, Beaudette, L.A, Cassidy, M.B, Leung, K.T, Hoang, T.A, Vogel, H.J, Trevors, J.T, Lee, H
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Cloning, Molecular
Humans
Hydrogen-Ion Concentration
Hydrolases - chemistry
Hydrolases - genetics
Hydrolases - metabolism
Hydroquinones - chemistry
Hydroquinones - metabolism
Molecular Sequence Data
Sequence Alignment
Sphingomonas - enzymology
Sphingomonas - genetics
Temperature
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Summary:Tetrachlorohydroquinone reductive dehalogenase (PcpC) is the second of three enzymes that catalyze the initial degradation of pentachlorophenol in Sphingomonas sp. UG30 and several other bacterial strains. The UG30 PcpC shares a high degree (94%) of primary sequence identity with the well-studied PcpC from Sphingobium chlorophenolicum ATCC 39723. Significant differences, however, were observed between the two PcpC enzymes in some of their functional and kinetic properties. The temperature optimum of the UG30 PcpC is 10 °C higher and the pH optimum is approximately 2 units higher than the S. chlorophenolicum PcpC. In addition, the S. chlorophenolicum PcpC is subject to inhibition by the substrate tetrachlorohydroquinone (TCHQ), and this has necessitated the use of a mutant enzyme, which was not inhibited by TCHQ, for kinetic studies. In contrast, the UG30 PcpC was not inhibited by TCHQ and this may allow detailed kinetic and mechanistic studies using the wild-type enzyme.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(02)02711-0