The structural interpretations of residue Ser297 in catalytic efficiency of Escherichia coli phenylalanine aminotransferase.
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.
Wu
Szu-Pei
SP
Institute of Biological Chemistry, Academia Sinica, 128, Academia Road Sec 2, Nankang, Taipei 115, Taiwan. szupeiwu@gate.sinica.edu.tw
Hwang
Tzann-Shun
TS
Ko
Tzu-Ping
TP
Wang
Andrew H-J
AH
Tsai
Hsin
H
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
D029968:Escherichia coli Proteins; D000637:Transaminases; C022340:phenylalanine aminotransferase