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Biochemical and structural studies of a l-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii

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Biochemical and structural studies of a l-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii. / Rye, Carrie A.; Isupov, Michail N.; Lebedev, Andrey A.; Littlechild, Jennifer A.

In: Extremophiles, Vol. 13, No. 1, 01.2009, p. 179-190.

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Harvard

Rye, CA, Isupov, MN, Lebedev, AA & Littlechild, JA 2009, 'Biochemical and structural studies of a l-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii', Extremophiles, vol. 13, no. 1, pp. 179-190. https://doi.org/10.1007/s00792-008-0208-0

APA

Rye, C. A., Isupov, M. N., Lebedev, A. A., & Littlechild, J. A. (2009). Biochemical and structural studies of a l-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii. Extremophiles, 13(1), 179-190. https://doi.org/10.1007/s00792-008-0208-0

Vancouver

Rye CA, Isupov MN, Lebedev AA, Littlechild JA. Biochemical and structural studies of a l-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii. Extremophiles. 2009 Jan;13(1):179-190. https://doi.org/10.1007/s00792-008-0208-0

Author

Rye, Carrie A. ; Isupov, Michail N. ; Lebedev, Andrey A. ; Littlechild, Jennifer A. / Biochemical and structural studies of a l-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii. In: Extremophiles. 2009 ; Vol. 13, No. 1. pp. 179-190.

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@article{d23bef9dc951461bb8e2e72c1cef0d87,
title = "Biochemical and structural studies of a l-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii",
abstract = "Haloacid dehalogenases have potential applications in the pharmaceutical and fine chemical industry as well as in the remediation of contaminated land. The l-2-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned and over-expressed in Escherichia coli and successfully purified to homogeneity. Here we report the structure of the recombinant dehalogenase solved by molecular replacement in two different crystal forms. The enzyme is a homodimer with each monomer being composed of a core-domain of a beta-sheet bundle surrounded by alpha-helices and an alpha-helical sub-domain. This fold is similar to previously solved mesophilic l-haloacid dehalogenase structures. The monoclinic crystal form contains a putative inhibitor l-lactate in the active site. The enzyme displays haloacid dehalogenase activity towards carboxylic acids with the halide attached at the C2 position with the highest activity towards chloropropionic acid. The enzyme is thermostable with maximum activity at 60A degrees C and a half-life of over 1 h at 70A degrees C. The enzyme is relatively stable to solvents with 25{\%} activity lost when incubated for 1 h in 20{\%} v/v DMSO.",
keywords = "Haloacid dehalogenase, Sulfolobus tokodaii, X-ray structure, XANTHOBACTER-AUTOTROPHICUS GJ10, L-2-HALOACID DEHALOGENASE, REACTION-MECHANISM, CRYSTAL-STRUCTURES, PSEUDOMONAS SP, MICROBES, PROTEINS, PROGRAM, ENZYME, YL",
author = "Rye, {Carrie A.} and Isupov, {Michail N.} and Lebedev, {Andrey A.} and Littlechild, {Jennifer A.}",
year = "2009",
month = "1",
doi = "10.1007/s00792-008-0208-0",
language = "English",
volume = "13",
pages = "179--190",
journal = "Extremophiles",
issn = "1431-0651",
publisher = "Springer Japan",
number = "1",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Biochemical and structural studies of a l-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii

AU - Rye, Carrie A.

AU - Isupov, Michail N.

AU - Lebedev, Andrey A.

AU - Littlechild, Jennifer A.

PY - 2009/1

Y1 - 2009/1

N2 - Haloacid dehalogenases have potential applications in the pharmaceutical and fine chemical industry as well as in the remediation of contaminated land. The l-2-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned and over-expressed in Escherichia coli and successfully purified to homogeneity. Here we report the structure of the recombinant dehalogenase solved by molecular replacement in two different crystal forms. The enzyme is a homodimer with each monomer being composed of a core-domain of a beta-sheet bundle surrounded by alpha-helices and an alpha-helical sub-domain. This fold is similar to previously solved mesophilic l-haloacid dehalogenase structures. The monoclinic crystal form contains a putative inhibitor l-lactate in the active site. The enzyme displays haloacid dehalogenase activity towards carboxylic acids with the halide attached at the C2 position with the highest activity towards chloropropionic acid. The enzyme is thermostable with maximum activity at 60A degrees C and a half-life of over 1 h at 70A degrees C. The enzyme is relatively stable to solvents with 25% activity lost when incubated for 1 h in 20% v/v DMSO.

AB - Haloacid dehalogenases have potential applications in the pharmaceutical and fine chemical industry as well as in the remediation of contaminated land. The l-2-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned and over-expressed in Escherichia coli and successfully purified to homogeneity. Here we report the structure of the recombinant dehalogenase solved by molecular replacement in two different crystal forms. The enzyme is a homodimer with each monomer being composed of a core-domain of a beta-sheet bundle surrounded by alpha-helices and an alpha-helical sub-domain. This fold is similar to previously solved mesophilic l-haloacid dehalogenase structures. The monoclinic crystal form contains a putative inhibitor l-lactate in the active site. The enzyme displays haloacid dehalogenase activity towards carboxylic acids with the halide attached at the C2 position with the highest activity towards chloropropionic acid. The enzyme is thermostable with maximum activity at 60A degrees C and a half-life of over 1 h at 70A degrees C. The enzyme is relatively stable to solvents with 25% activity lost when incubated for 1 h in 20% v/v DMSO.

KW - Haloacid dehalogenase

KW - Sulfolobus tokodaii

KW - X-ray structure

KW - XANTHOBACTER-AUTOTROPHICUS GJ10

KW - L-2-HALOACID DEHALOGENASE

KW - REACTION-MECHANISM

KW - CRYSTAL-STRUCTURES

KW - PSEUDOMONAS SP

KW - MICROBES

KW - PROTEINS

KW - PROGRAM

KW - ENZYME

KW - YL

UR - http://www.scopus.com/inward/record.url?scp=58149194643&partnerID=8YFLogxK

U2 - 10.1007/s00792-008-0208-0

DO - 10.1007/s00792-008-0208-0

M3 - Article

VL - 13

SP - 179

EP - 190

JO - Extremophiles

JF - Extremophiles

SN - 1431-0651

IS - 1

ER -