The structural interpretations of residue Ser297 in catalytic efficiency of Escherichia coli phenylalanine aminotransferase

Szu Pei Wu, Tzann Shun Hwang, Tzu Ping Ko, Andrew H.J. Wang, Hsin Tsai

研究成果: 雜誌貢獻文章同行評審

1 引文 斯高帕斯(Scopus)

摘要

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.

原文英語
頁(從 - 到)390-394
頁數5
期刊Biochimica et Biophysica Acta - Proteins and Proteomics
1647
發行號1-2
DOIs
出版狀態已發佈 - 4月 11 2003
對外發佈

ASJC Scopus subject areas

  • 分析化學
  • 生物物理學
  • 生物化學
  • 分子生物學

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