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dc.contributor.authorManetas, G.
dc.contributor.authorStamatakis, K.
dc.contributor.authorSamaras, G.
dc.date.accessioned2015-07-11T17:33:36Z
dc.date.available2015-07-11T17:33:36Z
dc.date.issued1986
dc.identifier.otherdoi:10.1016/S0176-1617(86)80189-4
dc.identifier.urihttp://hdl.handle.net/123456789/608
dc.description.abstractThe rate of adenylate kinase activity from the C4 plant Saccharum ravenae at saturating substrate and Mg2+ concentrations is 7 times higher in the direction of ADP formation (AMP + ATP →2ADP) than in the reverse direction. At low Mg2+ the reverse reaction is faster than the forward. This is due to a strong positive cooperation with Mg2+ in the forward reaction, whereas the reverse reaction follows a normal hyperbolic rate curve. Kinetic properties of the enzyme are the same at either 7.2 or 7.8 pH values. Positive cooperation with Mg2+ is also observed in adenylate kinase extracted from Zea mays, A triplex halimus and Cyperus rotundus (C4 plants) as well as from Kalanchoe tubiflora and Agave americana (CAM plants of the malic enzyme decarboxylation pathway). It is suggested that the enzyme might be regulated through the diurnal changes in stromal Mg2+ concentrations.el
dc.language.isoenel
dc.subjectAdenylate kinaseel
dc.subjectC4el
dc.subjectCAMel
dc.subjectMg2+ regulationel
dc.titleMg2+-Regulation of C4 and CAM Adenylate Kinaseel
dc.typeArticleel


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