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Identification of the functional improtance of valine‐19 residue in streptokinase by N‐terminal deletion and site‐directed mutagenesis
Author(s) -
Lee Si Hyoung,
Jeong Seong Tae,
Kim Il Chul,
Byun Si Myung
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700201201
Subject(s) - streptokinase , site directed mutagenesis , residue (chemistry) , mutagenesis , chemistry , plasminogen activator , amino acid , valine , biochemistry , active site , microbiology and biotechnology , biology , mutation , mutant , enzyme , genetics , gene , medicine , myocardial infarction
Streptokinase (SK) is a bacterial plasminogen activator of multi‐domain structure. In deletion analysis of the N‐terminal region of SK, the deletion of 20 amino acids (SKΔN20) resulted in the dramatic reduction of plasminogen activator activity compared to deletion of 7 (SK ΔN7) and 13 amino acids (SKΔN13). The incubation time to reach maximal active site generation in an equimolar mixture of SKΔN20 and plasminogen was the same as that for wild‐type SK. To identify the functional residues important in plasminogen activation, several site‐directed mutations were introduced at the region spanning Serl6‐Val20 of SK. The results showed that Vall9 residue is important for the activity of the SK‐plasminogen complex.