Competition of Pyridoxal 5'-Phosphate with Ribulose 1,5-Bisphosphate and Effector Sugar Phosphates at the Reaction Centers of the Spinach Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase
dc.contributor.author | Vater, Joachim | |
dc.contributor.author | Gaudszun, Thomas | |
dc.contributor.author | Scharnow, Harald | |
dc.contributor.author | Salnikow, Johann | |
dc.date.accessioned | 2019-01-04T13:17:37Z | |
dc.date.available | 2019-01-04T13:17:37Z | |
dc.date.issued | 1980 | |
dc.description.abstract | The 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. | en |
dc.identifier.eissn | 1865-7125 | |
dc.identifier.issn | 0939-5075 | |
dc.identifier.uri | https://depositonce.tu-berlin.de/handle/11303/8805 | |
dc.identifier.uri | http://dx.doi.org/10.14279/depositonce-7934 | |
dc.language.iso | en | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/3.0/ | |
dc.subject.ddc | 570 Biowissenschaften; Biologie | de |
dc.subject.other | ribulose 1,5-bisphosphate carboxylase/oxygenase | en |
dc.subject.other | effector studies | en |
dc.subject.other | pyridoxal 5'-phosphate inhibition | en |
dc.title | Competition of Pyridoxal 5'-Phosphate with Ribulose 1,5-Bisphosphate and Effector Sugar Phosphates at the Reaction Centers of the Spinach Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase | en |
dc.type | Article | en |
dc.type.version | publishedVersion | en |
dcterms.bibliographicCitation.doi | 10.1515/znc-1980-5-611 | |
dcterms.bibliographicCitation.issue | 5-6 | |
dcterms.bibliographicCitation.journaltitle | Zeitschrift fĂĽr Naturforschung C | de |
dcterms.bibliographicCitation.originalpublishername | De Gruyter | en |
dcterms.bibliographicCitation.originalpublisherplace | Berlin | |
dcterms.bibliographicCitation.pageend | 422 | |
dcterms.bibliographicCitation.pagestart | 416 | |
dcterms.bibliographicCitation.volume | 35 | |
tub.accessrights.dnb | free | |
tub.affiliation | Fak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Physikalische Chemie / Biophysikalische Chemie | de |
tub.affiliation.faculty | Fak. 2 Mathematik und Naturwissenschaften | de |
tub.affiliation.group | FG Physikalische Chemie / Biophysikalische Chemie | de |
tub.affiliation.institute | Inst. Chemie | de |
tub.publisher.universityorinstitution | Technische Universität Berlin | de |
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