title: The structural interpretations of residue Ser297 in catalytic efficiency of Escherichia coli phenylalanine aminotransferase.
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.
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, 128, Academia Road Sec 2, Nankang, Taipei 115, Taiwan. szupeiwu@gate.sinica.edu.tw
authors.forename: Szu-Pei
authors.initials: SP
authors.lastname: Wu
authors.forename: Tzann-Shun
authors.initials: TS
authors.lastname: Hwang
authors.forename: Tzu-Ping
authors.initials: TP
authors.lastname: Ko
authors.forename: Andrew H-J
authors.initials: AH
authors.lastname: Wang
authors.forename: Hsin
authors.initials: H
authors.lastname: Tsai
mesh_terms: D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D007700:Kinetics; D013329:Structure-Activity Relationship; D000637:Transaminases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D000637:Transaminases; C022340:phenylalanine aminotransferase