Simmaco M, John R A, Barra D, Bossa F
FEBS Lett. 1986 Apr 7;199(1):39-42. doi: 10.1016/0014-5793(86)81219-4.
Tentative assignments of functional residues in rat liver mitochondrial ornithine aminotransferase have recently been made using the amino acid sequence deduced from a cDNA clone [(1985) J.Biol.Chem. 260, 12993-12997]. Partial sequences obtained using the pure mature protein demonstrate that one of these assignments, that of Lys 292 as the residue that binds the coenzyme pyridoxal phosphate, is correct. However, the identification of the Glu 34-Gln 35 bond as the site of post-translational proteolysis is in error. This cleavage occurs instead at Ala 25-Thr 26.
最近，利用从一个cDNA克隆推导出来的氨基酸序列，对大鼠肝脏线粒体鸟氨酸转氨酶中的功能残基进行了初步定位[（1985年）《生物化学杂志》260, 12993 - 12997]。使用纯成熟蛋白获得的部分序列表明，这些定位之一，即将赖氨酸292鉴定为结合辅酶磷酸吡哆醛的残基，是正确的。然而，将谷氨酸34 - 谷氨酰胺35键鉴定为翻译后蛋白水解位点是错误的。这种切割实际上发生在丙氨酸25 - 苏氨酸26处。
