6533b7d6fe1ef96bd1265a9b

RESEARCH PRODUCT

Intracellular compartmentation and regulation of two shikimate dehydrogenase isoenzymes in Pisum sativum

Gunter M. Rothe

subject

Shikimate dehydrogenaseGeneral MedicineBiologybiology.organism_classificationMolecular biologyIsozymePisumchemistry.chemical_compoundCytosolchemistryBiochemistryAnthranilic acidMicrobodyGallic acidPolyacrylamide gel electrophoresis

description

Summary Pea seeds as well as sprouts and roots contain two isoenzymes of shikimate dehydrogenase. Both isoenzymes can be separated by Polyacrylamide gel electrophoresis as well as through ammonium sulfate fractionation. The molecular weight of both isoenzymes are the same although the net electric charge is different. The Km value for isoenzyme 1 is 3,5 × 10 −4 and the Km value for isoenzyme 2 is 1,67 × 10 −4 M. 3,4-dihydroxybenzoic acid, 3,5-dihydroxybenzoic acid, gallic acid, anthranilic acid and p-methoxycinnamic acid inhibited both isoenzymes competitively. Anthranlic acid showed the largest affinity to both isoenzymes. M-methoxycinnamic acid and m-nitrocinnamic acid inhibited both isoenzymes non-com-petitively. Isoenzyme 2 was always less inhibited than isoenzyme 1. Isoenzyme 1 could be located in the microbodies while isoenzyme 2 could be located in the cytosol.

https://doi.org/10.1016/s0044-328x(74)80168-6