Article ; Online: Important amino acid residues of hexachlorocyclohexane dehydrochlorinases (LinA) for enantioselective transformation of hexachlorocyclohexane isomers.
2017 Volume 28, Issue 2-3, Page(s) 171–180
Abstract: LinA-type1 and LinA-type2 are two well-characterized variants of the enzyme 'hexachlorocyclohexane ... and T133) in LinA-type1 that could be involved in selective binding of the substrates. Experimental ... in LinA-type1, i.e. K20Q, L96C, and A131G, caused a reversal in its preference ...
Abstract | 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 α-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 α-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 δ-HCH, and β-, γ-, and δ-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. |
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MeSH term(s) | Amino Acids/chemistry ; Biodegradation, Environmental ; Chromatography, Gas ; Lindane/chemistry ; Lindane/metabolism ; Lyases/chemistry ; Lyases/genetics ; Lyases/metabolism ; Mutant Proteins/metabolism ; Mutation/genetics ; Stereoisomerism ; Structure-Activity Relationship |
Chemical Substances | Amino Acids ; Mutant Proteins ; alpha-hexachlorocyclohexane (319-84-6) ; delta-hexachlorocyclohexane (319-86-8) ; Lindane (59NEE7PCAB) ; Lyases (EC 4.-) ; dehydrochlorinases (EC 4.5.-) |
Language | English |
Publishing date | 2017-06 |
Publishing country | Netherlands |
Document type | Journal Article |
ZDB-ID | 1056014-2 |
ISSN | 1572-9729 ; 0923-9820 |
ISSN (online) | 1572-9729 |
ISSN | 0923-9820 |
DOI | 10.1007/s10532-017-9786-9 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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