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Cysteine reactivity in sorbitol and aldehyde dehydrogenases Differences towards the pattern in alcohol dehydrogenase
Author(s) -
Johansson Jan,
Fleetwood Louise,
Jörnvall Hans
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80464-r
Subject(s) - sorbitol dehydrogenase , sorbitol , cysteine , aldehyde dehydrogenase , alcohol dehydrogenase , reactivity (psychology) , alcohol , biochemistry , chemistry , aldehyde , dehydrogenase , enzyme , organic chemistry , medicine , catalysis , alternative medicine , pathology
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.