Kinetic properties of the glucose-6-phosphate and 6 phosphogluconate dehydrogenases from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo
作者： Bernd Moritz , Katharina Striegel , Albert A. de Graaf , Hermann Sahm
DOI: 10.1046/J.1432-1327.2000.01354.X
关键词: Erythrose 、 Product inhibition 、 Glucose 6-phosphate 、 Corynebacterium glutamicum 、 Dehydrogenase 、 Biology 、 Biochemistry 、 Pentose phosphate pathway 、 Ribulose 、 NAD+ kinase
摘要: The glucose-6-phosphate (Glc6P) and 6-phosphogluconate (6PG) dehydrogenases of the amino-acid-producing bacterium Corynebacterium glutamicum were purified to homogeneity kinetically characterized. Glc6P dehydrogenase was a heteromultimeric complex, which consists Zwf OpcA subunits. product inhibition pattern consistent with an ordered bi-bi mechanism. 6PG found operate according Theorell-Chance bi-ter Both enzymes inhibited by NADPH additionally ATP, fructose 1,6-bisphosphate (Fru1,6P2), D-glyceraldehyde 3-phosphate (Gra3P), erythrose 4-phosphate ribulose 5-phosphate (Rib5P). considered be most important, constants around 25 microM for both enzymes. Intracellular metabolite concentrations determined in two isogenic strains C. plasmid-encoded NAD- NADP-dependent glutamate dehydrogenases. NADP+ levels between 130 290 microM, is very much higher than respective Km Ki values. concentration 500 strains. vivo fluxes through oxidative part pentose phosphate pathway calculated on basis intracellular kinetic vitro agreement same NMR after 13C-labelling. From derived model thus validated, it concluded that mainly regulated ratio specific enzyme activities
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