Alteration of the specificity of ecotin, an E. coli serine proteinase inhibitor, by site directed mutagenesis.

Abstract:

:The gene of ecotin, an E. coli proteinase inhibitor, was cloned, and by site-directed mutagenesis the active site residue of the protein, Met84, was mutated to Lys, Arg and Leu. The recombinant wild-type and mutant inhibitors were overexpressed in E. coli, purified to homogeneity and their inhibitory effects on trypsin, chymotrypsin and elastase were compared. Of these serine proteinases trypsin is the most strongly inhibited by wild type ecotin and its mutants. According to our results the character of residue 84 of ecotin significantly but not dramatically modifies the specificity of the inhibitor.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Pál G,Sprengel G,Patthy A,Gráf L

doi

10.1016/0014-5793(94)80584-9

subject

Has Abstract

pub_date

1994-03-28 00:00:00

pages

57-60

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)80584-9

journal_volume

342

pub_type

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