Journal of Biological Chemistry · 1971 · 76 citations · 24 references
Life SciencesBiochemistryEnzyme MechanismEnzymologyPhotosynthesisChloroplast BiochemistryEnzyme InhibitionEnzyme KineticsEnzyme RegulationPhotosynthesis BiochemistryPlant EnzymesElectrophoresisEnzyme ActivityEnzyme Activity RegulationEnzymesMolecular Weight DeterminationPorphyrin Pathway EnzymesSpecific Activity Determination
Abstract δ-Aminolevulinic acid synthase has been purified 1300-fold from photosynthetically cultured Rhodopseudomonas spheroides. The enzyme having a specific activity of 130 units per mg shows one major band and two minor bands upon disc electrophoresis. Some properties, including molecular weight, stability, and the inhibition of enzyme activity by hemin are reported. The comparative behavior of crude and purified enzyme toward oxidizing and reducing agents is discussed. Although δ-aminolevulinic acid synthase functions in a regulatory capacity, it apparently lacks some characteristics generally observed with allosteric enzymes.
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