PMID:6337636
| Citation |
Hayzer, DJ and Leisinger, T (1983) Proline biosynthesis in Escherichia coli. Kinetic and mechanistic properties of glutamate semialdehyde dehydrogenase. Biochim. Biophys. Acta 742:391-8 |
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| 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 Km for DL-pyrroline-5-carboxylic acid is 2.5 mM, for NADP+ is 0.05 mM and for phosphate is 0.35 mM. The Vmax 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 gamma-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. |
| Links | |
| Keywords |
Aldehyde Oxidoreductases/metabolism; Escherichia coli/enzymology; Glutamate-5-Semialdehyde Dehydrogenase; Kinetics; Mathematics; NADP; Proline/biosynthesis; Substrate Specificity |
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