Hempel J, von Bahr-Lindström H, Jörnvall H
Eur J Biochem. 1984 May 15;141(1):21-35. doi: 10.1111/j.1432-1033.1984.tb08150.x.
Analysis of CNBr fragments and other peptides from human liver cytoplasmic aldehyde dehydrogenase enabled determination of the complete primary structure of this protein. The monomer has an acylated amino terminus and is composed of 500 amino acid residues, including 11 cysteine residues. No evidence of any microheterogeneity was obtained, supporting the concept that the enzyme is a homotetramer . The disulfiram-sensitive thiol in the protein, earlier identified through its reaction with iodoacetamide, is contributed by a cysteine residue at position 302, while the cysteine which in horse liver mitochondrial aldehyde dehydrogenase is reactive with coenzyme analogs appears to correspond to either Cys-455 or Cys-463. Analysis of glycine distribution and prediction of secondary structures to localize beta alpha beta regions typical for coenzyme-binding are not fully unambiguous, but suggest a short region around position 245 as a likely segment for this function. In this region, sequence similarities to parts of a bacterial aspartate-beta-semialdehyde dehydrogenase and a mammalian alcohol dehydrogenase were noted. Otherwise, no extensive similarities were detected in comparisons with characterized mammalian enzymes of similar activity or subunit size as aldehyde dehydrogenase (glyceraldehyde-3-phosphate dehydrogenase and glutamate dehydrogenase, respectively).
对人肝细胞质醛脱氢酶的溴化氰片段和其他肽段进行分析，得以确定该蛋白质的完整一级结构。该单体具有一个酰化的氨基末端，由500个氨基酸残基组成，包括11个半胱氨酸残基。未获得任何微异质性的证据，支持该酶是同四聚体的概念。该蛋白质中对双硫仑敏感的巯基，早期通过其与碘乙酰胺的反应得以鉴定，由302位的一个半胱氨酸残基提供，而在马肝线粒体醛脱氢酶中与辅酶类似物反应的半胱氨酸似乎对应于Cys-455或Cys-463。对甘氨酸分布的分析以及对二级结构的预测，以定位辅酶结合典型的β-α-β区域，并不完全明确，但表明245位附近的一个短区域可能是该功能的片段。在该区域，注意到与细菌天冬氨酸-β-半醛脱氢酶和哺乳动物醇脱氢酶的部分序列相似性。否则，与具有相似活性或亚基大小的已表征哺乳动物酶（分别为甘油醛-3-磷酸脱氢酶和谷氨酸脱氢酶）进行比较时，未检测到广泛的相似性。
