Role of a repeated hexapeptide motif GIHFAP near C-terminus in assembly, stability, and activity of "HCH dehydrochlorinase LinA".
Ankit S Macwan, Nidhi Srivastava, Saleem Javed, Ashwani Kumar
Index: Appl. Biochem. Biotechnol. 169(4) , 1397-404, (2013)
Full Text: HTML
Abstract
Enzyme "hexachlorocyclohexane (HCH) dehydrochlorinase LinA" mediates first step of aerobic microbial degradation of a chlorinated insecticide γ-HCH. The archetypal LinA-type1 consists of 156 amino acids that include a directly repeated hexapeptide motif GIHFAP at positions 141-146 and 148-153. Analysis of a series of LinA mutants, containing none, one, two, or three units of this repeated motif revealed that two units, as present in wild-type LinA, are required for its optimal activity and stability. Moreover, the presence of a bend in its secondary structure due to a proline residue that precedes the distal repeated unit contributes to enhanced LinA activity.
Related Compounds
Related Articles:
2015-07-30
[Anal. Chim. Acta 886 , 56-65, (2015)]
2013-09-01
[Environ. Int. 59 , 485-93, (2013)]
2015-02-18
[J. Agric. Food Chem. 63(6) , 1839-48, (2015)]
2011-12-01
[J. Sci. Ind. Res. 65(10) , 808, (2006)]
Developing structure-activity relationships for the prediction of hepatotoxicity.
2010-07-19
[Chem. Res. Toxicol. 23 , 1215-22, (2010)]