Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme.
Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme.
复制标题
来自人肝脏的醛脱氢酶。
DOI：
--
复制
发表时间：
1984
期刊：
影响因子：
--
通讯作者：
H. Jörnvall
中科院分区：
文献类型：
--
作者：
J. Hempel;H. von Bahr;H. Jörnvall
CNBr片段和其他肽从人肝细胞质醛脱氢酶的分析，使这种蛋白质的完整的一级结构的测定。该单体具有酰化的氨基末端，由500个氨基酸残基组成，包括11个半胱氨酸残基。没有证据表明任何微观异质性，支持的概念，酶是一个同源四聚体。蛋白质中的双硫仑敏感性硫醇，早期通过其与碘乙酰胺的反应鉴定，由302位的半胱氨酸残基贡献，而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。甘氨酸分布的分析和二级结构的预测，以定位β-α-β区域典型的辅酶结合是不完全明确的，但建议一个短的区域周围的位置245作为一个可能的部分为这个功能。在这个区域，序列相似性的细菌谷氨酸-β-半醛脱氢酶和哺乳动物的醇脱氢酶的一部分。否则，没有广泛的相似性，检测到与特征的哺乳动物酶类似的活性或亚基大小的醛脱氢酶（甘油醛-3-磷酸脱氢酶和谷氨酸脱氢酶，分别）的比较。
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).
鉴定人肝细胞质醛脱氢酶（同工酶 E1）中含有反应性半胱氨酸残基的片段。
影响因子：
2.9
作者：
Hempel,J;Pietruszko,R;Fietzek,P;Jörnvall,H
通讯作者：
Jörnvall,H
通过与其他脱氢酶比较来预测 3-磷酸甘油脱氢酶的二级结构元件。
DOI：
10.1111/j.1432-1033.1980.tb04798.x
发表时间：
1980
期刊：
European journal of biochemistry
影响因子：
--
作者：
Otto,J;Argos,P;Rossmann,MG
通讯作者：
Rossmann,MG
人醛脱氢酶：改进的纯化程序以及同工酶 E1 和 E2 的比较。
DOI：
10.1111/j.1530-0277.1982.tb05001.x
发表时间：
1982
期刊：
Alcoholism, clinical and experimental research
影响因子：
--
作者：
Hempel,JD;Reed,DM;Pietruszko,R
通讯作者：
Pietruszko,R