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Weak activity of haloalkane dehalogenase LinB with 1,2,3-trichloropropane revealed by X-ray crystallography and microcalorimetry

Article Abstract:

The X-ray crystallography and microcalorimetry was used to demonstrate the detection of weak activity of Haloalkane dahalogenase LinB from Sphingobium japonicum with 1,2,3-trichloropropane (TCP). The observation showed LinB to be a useful starting material for the development of a new biocatalyst toward TCP by protein engineering, which could become increasingly important for engineering novel biocatalyst by using the scaffolds of proteins with promiscuous activities.

Author: Damborsky, Jiri, Nagata, Yuji, Prokop, Zbynek, Monincova, Marta, Vevodova, Jitka
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2007
Science & research, Biological Product (except Diagnostic) Manufacturing, Drugs, Biological Processors, Biocatalysts, Research, Usage, X-ray crystallography, Protein research

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Degradation of beta-hexachlorocyclohexane by haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26

Article Abstract:

A demonstration that the haloalkane dehalogenase LinB, to mediate the second step in the degradation of gamma-HCH in Sphingomonas paucimobilis UT26, metabolizes beta-Hexachlorocyclohexane (beta-HCH) to produce 2,3,4,5,6-pentachlorocyclohexanol is presented. The results suggested that, in the bacterial strain S. paucimobilis UT26, haloalkane dehalogenase LinB converts beta-HCH to PCHL.

Author: Damborsky, Jiri, Nagata, Yuji, Prokop, Zbynek, Tsuda, Masataka, Ohtsubo, Yoshiyuki, Sato, Yukari, Jerabek, Petr, Kumar, Ashwani
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
Pesticide and Other Agricultural Chemical Manufacturing, Agricultural chemicals, not elsewhere classified, Lindane, Biodegradation, Halogenation

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Reconstruction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB

Article Abstract:

Protein analysis reveals that 6 to 19 amino acids that form active site and entrance tunnel differ between LinB haloalkane dehalogenase from Sphingomonas paucimobilis and Rv2579 mycobacterium tuberculosis dehalogenase. By amino acid substitution the active sites of these two proteins are interchangeable.

Author: Damborsky, Jiri, Nagata, Yuji, Prokop, Zbynek, Marvanova, Sona, Sykorova, Jana, Monincova, Marta, Tsuda, Masataka
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
Japan, Czech Republic, Enzymes, Binding sites (Biochemistry), Active sites (Biochemistry), Enzyme structure-activity relationships, Amino acid structure-activity relationships, Substitution reactions

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Subjects list: Analysis
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