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B6db references: 6378205

type Journal Article
authors Kondo K, Wakabayashi S, Yagi T, Kagamiyama H.
title The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes
journal Biochem Biophys Res Commun
sel selected
ui 6378205
year (1984)
volume 122
number 1
pages 62-7
keywords Amino Acid Sequence
abstract The amino acid sequence of aspartate aminotransferase from E. coli B was determined by the alignment of seven cyanogen bromide peptides. The established sequence of the subunit was composed of 396 amino acid residues, and the molecular weight was calculated to be 43,573. The sequence was compared with those of the pig cytoplasmic and mitochondrial isoenzymes, showing that nearly 30% of all residues were invariant and that the E. coli enzyme exhibited the same degree of homology (about 40%) with either of them. Although majority of the residues were substituted, the functional residues constituting the active site structure were conserved.
last changed 2007/10/23 13:23

B6db references