Open AccessFormation and Reduction of Intermediate Acyladenylate by Aryl‐Aldehyde
Author(s) -
Gross Georg G.
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb02569.x
Subject(s) - chemistry , aldehyde , oxidoreductase , hydroxylamine , enzyme , aryl , catalysis , stereochemistry , medicinal chemistry , organic chemistry , alkyl
The enzyme aryl‐aldehyde: NADP oxidoreductase catalyzes a rapid exchange of PPi and ATP. The reaction requires the presence of an aromatic acid and Mg 2+ ions. The exchange reaction has a pH‐optimum of approx. 8.5 and is inhibited by NADPH. The inhibition of the exchange reaction by hydroxylamine as well as the enzymic formation of benzoylhydroxamate confirm that an activated intermediate is involved in the reduction of aromatic acids. This compound was identified as acyladenylate which, however, is assumed not to exist in the free state under normal conditions. In a subsequent step the acyladenylate is reduced to aldehyde. This reaction depends on the presence of sulfhydryls and does not require Mg 2+ ions. Both the activating and the reductive step are catalyzed by one enzyme.