Disease relevance of tyrB

• Purification and properties of aromatic amino acid aminotransferase from Klebsiella aerogenes [1].
• One mutation, designated tyrB, lies at about 80 min on the E. coli map and inactivates the "tyrosine-repressible" tyrosine/phenylalanine aminotransferase [2].
• The gene for aromatic amino acid aminotransferase (ArAT) from Paracoccus denitrificans was cloned, sequenced, and overexpressed in Escherichia coli cells [3].

High impact information on tyrB

• Enzyme A is identical in substrate specificity with transaminase A and is mainly an aspartate aminotransferase; enzyme B has never been described before and is an aromatic amino acid aminotransferase [4].
• Analysis of the substrate-recognition mode of aromatic amino acid aminotransferase by combined use of quasisubstrates and site-directed mutagenesis: systematic hydroxy-group addition/deletion studies to probe the enzyme-substrate interactions [5].
• Chromosomal fragments cloned because they complemented this mutation were found to complement leu mutations, and vice versa, but none of these fragments complemented a tyrB mutation [6].
• Role of the Escherichia coli aromatic amino acid aminotransferase in leucine biosynthesis [7].
• Mapping of the aspartate and aromatic amino acid aminotransferase genes tyrB and aspC [8].

Chemical compound and disease context of tyrB

• Escherichia coli aspartate aminotransferase (AspAT) and E. coli aromatic amino acid aminotransferase (AroAT) have almost identical and high activities toward acidic amino acid substrates [9].
• The Schiff base formed between Lys258 of Escherichia coli aromatic amino acid aminotransferase (ArAT) and the coenzyme pyridoxal 5'-phosphate (PLP) has a pKa value of 6.65 [10].

Biological context of tyrB

• Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene [11].
• The coding region of the tyrB gene and the deduced amino acid sequence revealed that the aromatic amino acid aminotransferase of E. coli is homologous with the aspartate aminotransferase [11].
• Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: modulation by binding of ligands and implications for its role in catalysis [10].
• We found a gene homologous to tyrB, which encodes aromatic amino acid aminotransferase (ArAT, EC2.6.1.57) in Escherichia coli, in the genome of Salmonella typhimurium IFO 13245 [12].

Associations of tyrB with chemical compounds

• The presence of leucine increased the generation time of these cells and decreased the specific activity of the aromatic amino acid aminotransferase [7].

References