The structural interpretations of residue Ser297 in catalytic efficiency of Escherichia coli phenylalanine aminotransferase
Resource
Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 1647 (1-2): 390-394
Journal
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics
Pages
390-394
Date Issued
2003
Date
2003
Author(s)
Wu, Szu-Pei
Hwang, Tzann-Shun
Ko, Tzu-Ping
Wang, Andrew H. -J.
Tsai, Hsin
Abstract
Escherichia coli phenylalanine aminotransferase (ecPheAT) catalyzes the biosynthesis of phenylalanine and tyrosine. The crystal structure of ecPheAT was determined in our previous study. The comparison of the 3-D structure of several aminotransferases revealed that the residue at position 297 plays an important role in enzyme function. Analysis of activities and kinetic parameters of wild type and mutant ecPheATs suggested that the residue Ser(297) was structurally selected for better catalytic efficiency. Computational modeling of ecPheAT mutants further suggested that Ser in position 297 could make ecPheAT easy with change of conformation from open form to closed form.
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