Abstract
Homogeneous pantoate dehydrogenase ( d-pantoate:NAD + 4-oxidoreductase, EC 1.1.1.106) was shown to be sensitive to inactivation by p- chloromercuribenzoate (100 μM), 5,5−dithiobis(2-nitrobenzoic acid) (1 mM), iodoacetic acid (1 mM) and phenylglyoxal (5.3 mM). Potassium d-pantoate and NAD protected against inactivation by p- chloromercuribenzoate , 5,5′-dithiobis(2-nitrobenzoic acid) and iodoacetic acid. NAD and d-pantoate also provided substantial protection against inactivation by phenylglyoxal. Titration of the sulphydryl groups by 5,5′-dithiobis(2-nitrobenzoic acid) and incorporation of [ 14C]carboxymethyl revealed that there are two cysteine residues which are modified and one of those is essential for activity. In the presence of NAD and d-pantoate, incorporation of [ 14C]phenylglyoxal was decreased by 0.42 mol/mol of subunit.
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