Kondo K, Wakabayashi S, Yagi T, Kagamiyama H
Biochem Biophys Res Commun. 1984 Jul 18;122(1):62-7. doi: 10.1016/0006-291x(84)90439-x.
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.
通过对七条溴化氰肽段进行比对，确定了大肠杆菌B中天冬氨酸转氨酶的氨基酸序列。所确定的亚基序列由396个氨基酸残基组成，计算得到的分子量为43,573。将该序列与猪细胞质和线粒体同工酶的序列进行比较，结果表明所有残基中近30%是不变的，并且大肠杆菌酶与它们中的任何一种都具有相同程度的同源性（约40%）。尽管大多数残基发生了取代，但构成活性位点结构的功能性残基是保守的。
