Improving the Catalytic Activity of Phenylalanine Aminotransferase of Escherichia coli by Site‐Specific Mutation

Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase

“…PL promoter. The resulting plasmid was designated pTC3 (Wu et al, 1998). For overexpression of the tyrB gene, E. coli N4830-1 (Pharmacia, Uppsala), which contains a temperaturesensitive !…”

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

“…The E. coli tyrB gene coding for the phenylalanine aminotransferase [5] was subcloned from pTC3 [1] into the plasmid pCYB1 between sites of NdeI and XhoI to generate the plasmid pCY3. PCR overlap-extension mutagenesis technique [13] was used to construct the sitespecific mutants.…”

“…Phenylalanine aminotransferase (PheAT, EC 2.6.1.57), also called aromatic aminotransferase (ArAT) or tyrosine aminotransferase (TyrAT), is a pyridoxal 5V -phosphate (PLP)-dependent enzyme and is a key enzyme involved in the biosynthesis of phenylalanine and tyrosine. Escherichia coli PheAT (ecPheAT) possesses a broad substrate specificity and catalyzes the transamination reaction using either aromatic or dicarboxylic amino acid as the amino donor [1]. The enzyme is valuable in industry to produce some aromatic amino acids and their analogues, such as homophenylalanine, a starting material for synthesizing angiotension-converting enzyme inhibitor [2].…”