l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1

l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1 is a stereospecific enzyme that acts exclusively on l-isomers of 2-chloropropionate and dichloroacetate. The amino acid sequence of this enzyme is substantially different from those of other l-specific dehalogenases produced by other organisms....

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Detalles Bibliográficos
Autores principales: Adamu, Aliyu, Wahab, Roswanira Abdul, Huyop, Fahrul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer International Publishing 2016
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4899344/
https://www.ncbi.nlm.nih.gov/pubmed/27347470
http://dx.doi.org/10.1186/s40064-016-2328-9
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author Adamu, Aliyu
Wahab, Roswanira Abdul
Huyop, Fahrul
author_facet Adamu, Aliyu
Wahab, Roswanira Abdul
Huyop, Fahrul
author_sort Adamu, Aliyu
collection PubMed
description l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1 is a stereospecific enzyme that acts exclusively on l-isomers of 2-chloropropionate and dichloroacetate. The amino acid sequence of this enzyme is substantially different from those of other l-specific dehalogenases produced by other organisms. DehL has not been crystallised, and hence its three-dimensional structure is unavailable. Herein, we review what is known concerning DehL and tentatively identify the amino acid residues important for catalysis based on a comparative structural and sequence analysis with well-characterised l-specific dehalogenases.
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spelling pubmed-48993442016-06-24 l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1 Adamu, Aliyu Wahab, Roswanira Abdul Huyop, Fahrul Springerplus Review l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1 is a stereospecific enzyme that acts exclusively on l-isomers of 2-chloropropionate and dichloroacetate. The amino acid sequence of this enzyme is substantially different from those of other l-specific dehalogenases produced by other organisms. DehL has not been crystallised, and hence its three-dimensional structure is unavailable. Herein, we review what is known concerning DehL and tentatively identify the amino acid residues important for catalysis based on a comparative structural and sequence analysis with well-characterised l-specific dehalogenases. Springer International Publishing 2016-05-20 /pmc/articles/PMC4899344/ /pubmed/27347470 http://dx.doi.org/10.1186/s40064-016-2328-9 Text en © The Author(s). 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Review
Adamu, Aliyu
Wahab, Roswanira Abdul
Huyop, Fahrul
l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1
title l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1
title_full l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1
title_fullStr l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1
title_full_unstemmed l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1
title_short l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1
title_sort l-2-haloacid dehalogenase (dehl) from rhizobium sp. rc1
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4899344/
https://www.ncbi.nlm.nih.gov/pubmed/27347470
http://dx.doi.org/10.1186/s40064-016-2328-9
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