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The structural interpretations of residue Ser297 in catalytic efficiency of Escherichia coli phenylalanine aminotransferase
- Source :
-
BBA - Proteins & Proteomics . Apr2003, Vol. 1647 Issue 1/2, p390. 5p. - Publication Year :
- 2003
-
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 Ser297 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. [Copyright &y& Elsevier]
- Subjects :
- *ESCHERICHIA coli
*PHENYLALANINE
*AMINOTRANSFERASES
*TYROSINE
Subjects
Details
- Language :
- English
- ISSN :
- 15709639
- Volume :
- 1647
- Issue :
- 1/2
- Database :
- Academic Search Index
- Journal :
- BBA - Proteins & Proteomics
- Publication Type :
- Academic Journal
- Accession number :
- 9444954
- Full Text :
- https://doi.org/10.1016/S1570-9639(03)00104-3