Modulation of quinate: NAD(+) oxidoreductase activity through reversible phosphorylation in carrot cell suspensions.

Abstract:

:Quinate: NAD(+) oxidoreductase (EC 1.1.1.24) from carrot cells was deactivated by incubating partially purified extract with MgCl2 at 30°C. The deactivation process was prevented by adding fluoride, a phosphatase inhibitor. Once inactivated, the enzyme could recover its initial activity on incubation with ATP-Mg either in combination with or not in combination with an exogenous protein kinase. (32)PO4 was incorporated into the purified enzyme when the cell cultures were supplemented with labeled phosphate in vivo. Moreover, (32)P from [γ-(32)P]ATP was incorporated into the reductase when the enzyme was reactivated in the presence of protein kinase. From these results, it is concluded that the activation-inactivation process is due to phosphorylation-dephosphorylation of quinate:NAD(+) oxidoreductase.

journal_name

Planta

journal_title

Planta

authors

Refeno G,Ranjeva R,Boudet AM

doi

10.1007/BF00387863

subject

Has Abstract

pub_date

1982-05-01 00:00:00

pages

193-8

issue

3

eissn

0032-0935

issn

1432-2048

journal_volume

154

pub_type

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