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5326081 
Journal Article 
Role of a repeated hexapeptide motif gihfap near c-terminus in assembly, stability, and activity of "hch dehydrochlorinase lina" 
Macwan, AS; Srivastava, N; Javed, S; Kumar, A 
2013 
Yes 
Applied Biochemistry and Biotechnology
ISSN: 0273-2289
EISSN: 1559-0291 
169 
4 
1397-1404 
English 
23315208 
WOS:000315269200025 
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. 
LinA; Hexachlorocyclohexane; Dehydrochlorinase; Repeated motif