Multiple conformations in solution of the maize C₄-phosphoenolpyruvate carboxylase isozyme.

ABSTRACT: The photosynthetic phosphoenolpyruvate carboxylase isozyme from C₄ plants (PEPC-C₄) has a complex allosteric regulation, involving positive cooperativity in binding the substrate phosphoenolpyruvate as well as positive and negative allosteric effectors. Besides the proposed R- and T-states, previous kinetic results suggested functionally relevant different R-states of the maize enzyme (ZmPEPC-C₄) elicited by PEP or its two kinds of activators, glucose 6-phosphate or glycine. To detect these different R-state conformations, we used as conformational probes the fluorescence of 8-anilino-1-naphthalene sulfonate (ANS), near-UV circular dichroism (CD) spectroscopy, and limited proteolysis by trypsin. Phosphoenolpyruvate and malate bin

SUBMITTER: Barreda-Huerta F 

PROVIDER: S-EPMC8637149 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature