Cysteine reactivity in sorbitol and aldehyde dehydrogenases Differences towards the pattern in alcohol dehydrogenase

FEBS Letters

Fleetwood, Louise¹  Johansson, Jan¹  Jörnvall, Hans¹ 

[1] Department of Chemistry I, Karolinska Institutet, S-104 01, Stockholm, Sweden

关键词: Dehydrogenase differences;    Reactive Cys residue;    Carboxymethylation;    Active site;    Sorbitol dehydrogenase;    Aldehyde dehydrogenase;   

DOI  :  10.1016/0014-5793(92)80464-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In sorbitol dehydrogenase only one cysteine residue, Cys-43, is reactive in both anionic buffer (phosphate) and zinc-liganding buffer (imidazole) upon carboxymethylation. This is in contrast to the situation in the structurally related liver alcohol dehydrogenase, with either of two alternative Cys residues being reactive, and is compatible with differences in zinc-binding and active site relationships between these two metalloenzymes. Unrelated aldehyde dehydrogenase, upon carboxamidomethylation, shows a third pattern, now less well defined but confirming the presence of a thiol function of Cys-302 close to the active site.

【 授权许可】

Unknown