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B6db references: 78214646

type Journal Article
authors Powell, J. T.; Morrison, J. F.
title The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli
journal Eur J Biochem
ui 78214646
year (1978)
volume 87
number 2
pages 391-400.
keywords Amino Acids/analysis
abstract A simple and convenient procedure is described for the isolation in good yield of two amino-transferases from various strains of Escherichia coli. On the basis of their substrate specificities one of the enzymes has been classified as an aromatic amino acid aminotransferase and the other as an aspartate aminotransferase, but both act on a wide range of substrates. Pyridoxal phosphate is bound more strongly to the aspartate aminotransferase than to the aromatic amino transferase which cannot be fully re-activated after removal of the prosthetic group. Both enzymes are composed of two subunits which appear to be identical.
last changed 2002/11/12 16:17

B6db references