Effect of Carbonic Anhydrase on the Activity of Ribulose Bisphosphate Carboxylase

Autor:	I. F. Bird, M. J. Cornelius, Alfred J. Keys
Rok vydání:	1980
Předmět:	chemistry.chemical_classification Phosphoglycerate kinase biology Physiology Chemistry Ribulose RuBisCO Substrate (chemistry) Plant Science Michaelis–Menten kinetics chemistry.chemical_compound Enzyme Biochemistry Carboxylation Carbonic anhydrase biology.protein
Zdroj:	Journal of Experimental Botany. 31:365-369
ISSN:	1460-2431 0022-0957
DOI:	10.1093/jxb/31.2.365
Popis:	At concentrations of C02 less than saturating, carbonic anhydrase (EC 4.2.1.1) stimulates the carboxylation of ribulose bisphosphate catalysed by ribulose bisphosphate carboxylase (EC 4.1.1.3.9) in vitro. This is not through any beneficial association of the two enzymes but is a consequence of the increased rate of conversion of HCOj ion to C02, the substrate for the carboxylation. Carbonic anhydrase should always be included in reaction mixtures used to determine the Michaelis constant of ribulose bisphosphate carboxylase for C02 where fixation of radioactive C02 into phosphoglycerate is the basis of rate estimation. The effect is to decrease the value obtained for the Michaelis constant.
Databáze:	OpenAIRE
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