Inactivation of maize phosphoenolpyruvate carboxylase by urea.

Abstract:

:Phosphoenolpyruvate carboxylase purified from leaves of maize (Zea mays, L.) is sensitive to the presence of urea. Exposure to 2.5 m urea for 30 min completely inactivates the enzyme, whereas for a concentration of 1.5 m urea, about 1 h is required. Malate appears to have no effect on inactivation by urea of phosphoenolpyruvate carboxylase. However, the presence of 20 mm phosphoenolpyruvate or 20 mm glucose-6-phosphate prevents significant inactivation by 1.5 m urea for at least 1 h. The inactivation by urea is reversible by dilution. The inhibition by urea and the protective effects of phosphoenolpyruvate and glucose-6-phosphate are associated with changes in aggregation state.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Wedding RT,Dole P,Chardot TP,Wu MX

doi

10.1104/pp.100.3.1366

subject

Has Abstract

pub_date

1992-11-01 00:00:00

pages

1366-8

issue

3

eissn

0032-0889

issn

1532-2548

journal_volume

100

pub_type

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