Vater, JoachimGaudszun, ThomasScharnow, HaraldSalnikow, Johann2019-01-042019-01-0419800939-5075https://depositonce.tu-berlin.de/handle/11303/8805http://dx.doi.org/10.14279/depositonce-7934The Stimulation of the carboxylase reaction by effectors of ribulose 1,5-bisphosphate carboxyl­ ase/oxygenase displays higher sensitivity towards pyridoxal 5'-phosphate inhibition than the catalytical process itself. Pyridoxal 5'-phosphate binding to the enzyme is not affected by the modulators 6-phospho-gluconate and fructose 1,6-bisphosphate at low concentrations at which these agents stimulate the carboxylation rate. At higher concentrations these sugar phosphates protect the enzyme against pyridoxal 5'-phos-phate inhibition in a similar fashion like the substrate ribulose 1,5-bisphosphate. Such protection experiments in combination with spectrophotometrical studies of pyridoxal 5'-phosphate binding demonstrate two binding states of ribulose 1,5-bisphosphate at the reaction centers of the enzyme with different requirements for Mg2+. 6-Phosphogluconate functions as protector only in the presence of Mg2+. Our results imply a competition between pyridoxal 5'-phosphate and substrate or effector sugar phosphates at the reaction centers of the spinach carboxylase. It is proposed that the pyridoxal 5'-phosphate inhibition of the stimulatory activity of these effectors originates from a modification of the regulatory sites of the enzyme caused by pyridoxal 5'-phosphate binding to the catalytical sites.en570 Biowissenschaften; Biologieribulose 1,5-bisphosphate carboxylase/oxygenaseeffector studiespyridoxal 5'-phosphate inhibitionArticle1865-7125