Changes in NADP+-linked isocitrate dehydrogenase during tomato fruit ripening

✍ Scribed by Fernando Gallardo; Susana Gálvez; Pierre Gadal; Francisco M. Cánovas

• Publisher: Springer-Verlag
• Year: 1995
• Tongue: English
• Weight: 943 KB
• Volume: 196
• Category: Article
• ISSN: 0032-0935
• DOI: 10.1007/bf00193228

✦ Synopsis

The activaty of NADP+-specific isocitrate dehydrogenase (NADP +-IDH, EC 1.1.1.42) was investigated during the ripening of tomato (Lycopersicon esculenturn Mill.) fruit. In the breaker stage, NADP +-IDH activity declined but a substantial recovery was observed in the late ripening stages when most lycopene synthesis occurs. These changes resulted in higher NADP+-IDH activity and specific polypeptide abundance in ripe than in green fruit pericarp. Most of the enzyme corresponded to the predominant cytosolic isoform which was purified from both green and ripe fruits. Fruit NADP+-IDH seems to be a dimeric enzyme having a subunit size of 48 kDa. The K m values of the enzymes from green and ripe pericarp for NADP +, isocitrate and Mg 2+ were not significantly different. The similar molecular and kinetic properties and chromatographic behaviour of the enzymes from the two kinds of tissue strongly suggest that the ripening process is not accompanied by a change in isoenzyme complement. The increase in NADP+-IDH in the late stage of ripening also suggests that this enzyme is involved in the metabolism of C6 organic acids and in glutamate accumulation in ripe tissues.