Kinetic properties of UDP-glucose dehydrogenase from soybean nodules
1999; Elsevier BV; Volume: 147; Issue: 2 Linguagem: Inglês
10.1016/s0168-9452(99)00110-7
ISSN1873-2259
AutoresDouglas C. Stewart, Les Copeland,
Tópico(s)Nematode management and characterization studies
ResumoThe kinetic and regulatory properties of UDP-glucose dehydrogenase (EC 1.1.1.22) from the host cytosol of soybean (Glycine max L. cv. Alabaster) root nodules have been investigated. The results of studies with inhibitors, together with results from previous initial velocity studies (D.C. Stewart, L. Copeland, Plant Physiol. 116 (1998) 349–355), were consistent with a mechanism that does not have a central complex in which all of the substrates are bound simultaneously. Studies on the effect of pH on kinetic constants, and with p-chloromercuribenzoate, indicated that a sulfhydryl group was involved in substrate binding. UDP-xylose was a potent inhibitor of UDP-glucose dehydrogenase and is suggested to be involved in the fine control of activity through feedback inhibition. The values of kinetic parameters indicate that activity of purified UDP-glucose dehydrogenase was influenced by the ratio of NAD+/NADH.
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