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Important amino acid residues of hexachlorocyclohexane dehydrochlorinases (LinA) for enantioselective transformation of hexachlorocyclohexane isomers
Academic Science and Innovat Research, India; CSIR Indian Institute Toxicol Research, India.
Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Medicine and Health Sciences.
Swiss Federal Institute Aquat Science and Technology Eawag, Switzerland.
Academic Science and Innovat Research, India; CSIR Indian Institute Toxicol Research, India.
2017 (English)In: Biodegradation, ISSN 0923-9820, E-ISSN 1572-9729, Vol. 28, no 2-3, 171-180 p.Article in journal (Refereed) Published
Abstract [en]

LinA-type1 and LinA-type2 are two well-characterized variants of the enzyme hexachlorocyclohexane (HCH)-dehydrochlorinase. They differ from each other at ten amino acid positions and exhibit differing enantioselectivity for the transformation of the (-) and (+) enantiomers of alpha-HCH. Amino acids responsible for this enantioselectivity, however, are not known. An in silico docking analysis identified four amino acids (K20, L96, A131, and T133) in LinA-type1 that could be involved in selective binding of the substrates. Experimental studies with constructed mutant enzymes revealed that a combined presence of three amino acid changes in LinA-type1, i.e. K20Q, L96C, and A131G, caused a reversal in its preference from the (-) to the (+) enantiomer of alpha-HCH. This preference was enhanced by the additional amino acid change T133 M. Presence of these four changes also caused the reversal of enantioselectivity of LinA-type1 for delta-HCH, and beta-, gamma-, and delta-pentachlorocyclohexens. Thus, the residues K20, L96, A131, and T133 in LinA-type1 and the residues Q20, C96, G131, and M133 in LinA-type 2 appear to be important determinants for the enantioselectivity of LinA enzymes.

Place, publisher, year, edition, pages
SPRINGER , 2017. Vol. 28, no 2-3, 171-180 p.
Keyword [en]
HCH dehydrochlorinase LinA; Enantioselectivity; alpha-HCH enantiomers
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-138269DOI: 10.1007/s10532-017-9786-9ISI: 000400932900005PubMedID: 28251436OAI: oai:DiVA.org:liu-138269DiVA: diva2:1109112
Available from: 2017-06-13 Created: 2017-06-13 Last updated: 2017-06-30

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