Escherichia coli aromatic amino acid aminotransferase: Characterization and comparison with aspartate aminotransferase

Biochemistry ◽  
1993 ◽  
Vol 32 (45) ◽  
pp. 12229-12239 ◽  
Author(s):  
Hideyuki Hayashi ◽  
Katsura Inoue ◽  
Toshihito Nagata ◽  
Seiki Kuramitsu ◽  
Hiroyuki Kagamiyama
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Aspartate Aminotransferase ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acid Aminotransferase

Site-directed mutagenesis of the aromatic amino acid aminotransferase of Escherichia coli

1989 ◽  
Vol 17 (1) ◽  
pp. 195-195
Author(s):  
MARTIN J. GARTLAND ◽  
MICHAEL G. HUNTER ◽  
IAN G. FOTHERINGHAM ◽  
GEOFFREY C. ROWLAND ◽  
ROBERT E. GLASS
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Aromatic Amino Acid Aminotransferase

scholarly journals Aspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase

1985 ◽  
Vol 232 (3) ◽  
pp. 689-695 ◽  
Author(s):  
P N Lowe ◽  
A F Rowe
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aspartate Aminotransferase ◽  
Aromatic Amino Acid ◽  
Trichomonas Vaginalis ◽  
Aromatic Amino Acids ◽  
Significant Activity ◽  
Irreversible Inhibitor ◽  
Competitive Substrate ◽  
Aromatic Amino Acid Aminotransferase

Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and characterized. It is a dimeric protein of overall Mr approx. 100000. Only a single isoenzyme was found in T. vaginalis. The overall molecular and catalytic properties have features in common with both the vertebrate cytoplasmic and mitochondrial isoenzymes. The purified aspartate aminotransferase from T. vaginalis showed very high rates of activity with aromatic amino acids as donors and 2-oxoglutarate as acceptor. This broad-spectrum activity was restricted to aromatic amino acids and aromatic 2-oxo acids, and no significant activity was seen with other common amino acids, other than with the substrates and products of the aspartate: 2-oxoglutarate aminotransferase reaction. Co-purification and co-inhibition, by the irreversible inhibitor gostatin, of the aromatic amino acid aminotransferase and aspartate aminotransferase activities, in conjunction with competitive substrate experiments, strongly suggest that a single enzyme is responsible for both activities. Such high rates of aromatic amino acid aminotransferase activity have not been reported before in eukaryotic aspartate aminotransferase.

scholarly journals Crystal structure of Aspergillus fumigatus AroH , an aromatic amino acid aminotransferase

2021 ◽  
Author(s):  
Sharon Spizzichino ◽  
Gioena Pampalone ◽  
Mirco Dindo ◽  
Agostino Bruno ◽  
Luigina Romani ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Aspergillus Fumigatus ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acid Aminotransferase
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