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B6db references: 81116977

type Journal Article
authors Paris, C. G.; Magasanik, B.
title Purification and properties of aromatic amino acid aminotransferase from Klebsiella aerogenes
journal J Bacteriol
ui 81116977
year (1981)
volume 145
number 1
pages 266-71.
keywords Amino Acids/isolation & purification
abstract We describe the complete purification of aromatic aminotransferase I, the enzyme responsible for the ability of Klebsiella aerogenes to use tryptophan and phenylalanine as sole sources of nitrogen, as well as the partial purification of aromatic aminotransferase IV. An examination of the properties of these enzymes revealed that aminotransferase I had much greater affinity for the aromatic amino acids than aminotransferase IV, explaining the essential role of aminotransferase I in the utilization of exogenously supplied aromatic amino acids. The properties of aminotransferase IV suggest that this enzyme is actually an aspartate aminotransferase (EC, corresponding to the product of the aspC gene of Escherichia coli.
last changed 2002/11/12 16:17

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