Role of a repeated hexapeptide motif GIHFAP near C-terminus in assembly, stability, and activity of "HCH dehydrochlorinase LinA"

Appl Biochem Biotechnol. 2013 Feb;169(4):1397-404. doi: 10.1007/s12010-012-0035-8. Epub 2013 Jan 12.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Chromatography, Gel
  • Enzyme Stability
  • Hexachlorocyclohexane / metabolism*
  • Lyases / chemistry*
  • Lyases / metabolism*
  • Molecular Sequence Data

Substances

  • Bacterial Proteins
  • Hexachlorocyclohexane
  • Lyases