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If the reaction proceeds via the highly unlikely route B, the enzyme may also be inactivated by 5 but with 2-oxo-3-pentenoic acid as a potential turnover product.
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14
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10144242568
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note
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A standard 1 mL assay was performed in 50 mM potassium phosphate buffer (pH 7.5) at 23 °C, containing substrate, 8-20 μg ACC deaminase, 125 μg of L-lactate dehydrogenase, and 0.1 μmol of NADH. Loss of NADH absorbance at 340 nm (ε 6220) was monitored. The unit of activity is defined as μmol of NADH consumption per minute. The kinetic parameters of inactivation were derived from plotting the apparent inactivation rate, obtained by incubating ACC deaminase (90 μg) with 5 of varied concentration (1-10 mM), versus inhibitor concentration.
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24
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0026699542
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Since ACC is the precursor of an essential phytohormone, ethylene, studies of the reaction catalyzed by ACC deaminase may also provide information for designing methods to control and regulate the ethylene biosynthetic process (Dong, G.; Fernandez-Maculet, J. C.; Yang, S. F. Proc. Nail. Acad. Sci. U.S.A. 1992, 89, 9789; Klee, H. J.; Hayford, M. B.; Kretzmer, K. A.; Barry, G. F.; Kishore, G. M. Plant Cell, 1991, 3. 1187).
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Dong, G.1
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25
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0026251608
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Since ACC is the precursor of an essential phytohormone, ethylene, studies of the reaction catalyzed by ACC deaminase may also provide information for designing methods to control and regulate the ethylene biosynthetic process (Dong, G.; Fernandez-Maculet, J. C.; Yang, S. F. Proc. Nail. Acad. Sci. U.S.A. 1992, 89, 9789; Klee, H. J.; Hayford, M. B.; Kretzmer, K. A.; Barry, G. F.; Kishore, G. M. Plant Cell, 1991, 3. 1187).
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Klee, H.J.1
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