Lipase and Its Modulator from Pseudomonas sp. Strain KFCC 10818: Proline-to-Glutamine Substitution at Position 112 Induces Formation of Enzymatically Active Lipase in the Absence of the Modulator
Pseudomonas fluorescens
DOI:
10.1128/jb.183.20.5937-5941.2001
Publication Date:
2002-07-27T10:01:09Z
AUTHORS (6)
ABSTRACT
A lipase gene, lipK, and a modulator limK, of Pseudomonas sp. strain KFCC 10818 have been cloned, sequenced, expressed in Escherichia coli. The limK gene is located immediately downstream the lipK gene. Enzymatically active was produced only presence effect LimK on expression similar to those subfamily I.1 I.2 lipase-specific foldases (Lifs). deduced amino acid sequence shares low homology (17 19%) with known Lifs, suggesting that distantly related species. Surprisingly, variant does not require for its correct folding isolated study investigate functional interaction between LipK LimK. When absence LimK, P112Q formed an enzyme displayed 63% activity wild-type These results suggest Pro(112) residue involved key step folding. We expect novel finding this may contribute future research efficient or refolding industrially important lipases mechanism
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