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.
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This work was supported by a grant from the Department of Biotechnology, Government of India. Ankit Macwan and Nidhi Srivastava thank the Council of Scientific and Industrial Research, India, for fellowship support.
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Macwan, A.S., Srivastava, N., Javed, S. et al. Role of a Repeated Hexapeptide Motif GIHFAP Near C-terminus in Assembly, Stability, and Activity of “HCH Dehydrochlorinase LinA”. Appl Biochem Biotechnol 169, 1397–1404 (2013). https://doi.org/10.1007/s12010-012-0035-8
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DOI: https://doi.org/10.1007/s12010-012-0035-8