Abstract
The kinetics of the NADP +- and phosphate-dependent oxidation of glutamic acid 5-semialdehyde are consistent with a rapid-equilibrium random order mechanism. The K m for dl-pyrroline-5-carboxylic acid is 2.5 mM, for NADP + is 0.05 mM and for phosphate is 0.35 mM. The V max is approx. 8.0 units per mg protein. The reaction is highly specific for the dl-pyrroline-5-carboxylic acid and NADP +, but a number of divalent anions can substitute for phosphate. NADPH is competitive with respect to all three substrates and an analog of γ-glutamyl phosphate, 3-(phosphonoacetylamido)- l-alanine, is competitive with respect to dl-pyrroline-5-carboxylic acid and non-competitive with respect to NADP + and phosphate, suggesting dead-end complex formation.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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