Hempel J, Kaiser R, Jörnvall H
FEBS Lett. 1984 Aug 6;173(2):367-73. doi: 10.1016/0014-5793(84)80807-8.
A C-terminal segment of mitochondrial human liver aldehyde dehydrogenase was characterized. The results prove that a central part of this segment largely but not completely agrees with a structure of a tryptic peptide previously reported for the same isoenzyme. This part corresponds to a segment that contains the exchanged residue in the functionally deficient Oriental variant of mitochondrial aldehyde dehydrogenase [(1984) Proc. Natl. Acad. Sci. USA 81, 258-261]. The data suggest important functions for the C-terminal region of aldehyde dehydrogenase, clarify previously inconsistent results, and establish this structure in the typical enzyme, including the position corresponding to the mutation in the functional variant.
对人肝脏线粒体醛脱氢酶的C末端片段进行了表征。结果证明，该片段的中央部分与先前报道的同一同工酶的胰蛋白酶肽结构在很大程度上但并非完全一致。这部分对应于一个片段，该片段包含线粒体醛脱氢酶功能缺陷型东方变体中发生交换的残基[(1984年)美国国家科学院院刊81, 258 - 261]。这些数据表明醛脱氢酶C末端区域具有重要功能，澄清了先前不一致的结果，并确定了典型酶中的这种结构，包括与功能变体中突变相对应的位置。
