Abstract
Maize (Zea mays L.) leaf phosphoenolpyruvate (PEP) carboxylase (PEPCase) (EC 4.1.1.31) showed a lag in activity when assayed after storage at 0-4 °C. The lag was promoted by high pH on storage (7.8 -8.5) and was observed over a range of assay pH (7.1 -8.5). Thermal reactivation of the cold-stored enzyme by assay temperature (18 °C) accounted for most of the hysteretic effect, but presence of PEP in the reaction mixture was required to completely eliminate the lag. Based on steady-state rates after the lag, stability of PEPCase in the cold was independent of protein concentration . It is suggested that low temperature and high pH induce a change in the oligomerization state of PEPCase, resulting in a less active but relatively stable form of the enzyme. The lag probably reflects a reversal of this process, promoted by assay temperature and presence of PEP.
QTL Mapping in Three Connected Populations Reveals a Set of Consensus Genomic Regions for Low Temperature Germination Ability in Zea mays L.
