Purification and Properties of the Aromatic Amino Acid Aminotransferase from Gramicidin S-Producing Bacillus brevis

1987 ◽  
Vol 101 (4) ◽  
pp. 871-878 ◽  
Author(s):  
Masayuki KANDA ◽  
Kazuko HORI ◽  
Toshitsugu KUROTSU ◽  
Setsuko MIURA ◽  
Yoshitaka SAITO
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Bacillus Brevis ◽  
Gramicidin S ◽  
Purification And Properties ◽  
Aromatic Amino Acid Aminotransferase

scholarly journals Purification and Properties of Branched Chain Amino Acid Aminotransferase from Gramicidin S-Producing Bacillus brevis.

1995 ◽  
Vol 41 (1) ◽  
pp. 51-60 ◽  
Author(s):  
Masayuki KANDA ◽  
Kazuko HORI ◽  
Toshitsugu KUROTSU ◽  
Katsuko OHGISHI ◽  
Tomoko HANAWA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bacillus Brevis ◽  
Gramicidin S ◽  
Branched Chain Amino Acid ◽  
Purification And Properties ◽  
Branched Chain

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

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

scholarly journals Purification and properties of α-galactosidases from Vicia faba seeds

1969 ◽  
Vol 113 (1) ◽  
pp. 49-55 ◽  
Author(s):  
P. M. Dey ◽  
J. B. Pridham
Keyword(s):  
Amino Acid ◽  
Vicia Faba ◽  
Aromatic Amino Acid ◽  
Gel Filtration ◽  
Disc Electrophoresis ◽  
Thermal Stabilities ◽  
Molecular Weights ◽  
Purification And Properties ◽  
Enzyme I ◽  
Carbohydrate Contents

Two forms of α-galactosidase, I and II, exist in Vicia faba seeds and these have been purified 3660- and 337-fold respectively. They behaved as homogeneous preparations when examined by ultracentrifugation, disc electrophoresis and gel filtration. The apparent molecular weights of enzymes I and II, as determined by gel filtration, were 209000 and 38000 respectively. The carbohydrate contents of enzymes I and II were 25% and 2·8% respectively, and the enzymes differed in their aromatic amino acid compositions. Enzyme I was split into six inactive subunits in the presence of 6m-urea. α-Galactosidases I and II showed different pH optima and Km and Vmax. values with p-nitrophenyl α-d-galactoside and raffinose as substrates, and also differed in their thermal stabilities.

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