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- W2063735296 abstract "d-β-Hydroxybutyrate dehydrogenase (d-3-hydroxybutyrate: NAD+ oxidoreductase, EC 1.1.1.30) is a lipid-dependent enzyme which has an absolute and specific rquirement for phosphatidylcholine for function. Chemical derivatization studies using 1,2-cyclohexanedione, an arginine-specific reagent, have been carried out on the purified enzyme devoid of lipid as well as on the enzyme reactivated with phospholipid. Cyclohexanedione inactivated the active enzyme-phospholipid complex and the lipid-free enzyme was rendered inactivatable by phospholipid. From kinetic studies and by direct chemical derivatization studies with [1-14C]cyclohexanedione, we find that incorporation of a single cyclohexanedione molecule per enzyme monomer resulted in complete loss of enzymic activity. The presence of NADH or NAD+, cofactors for the enzyme, offered no protection for the rate of inactivation. The substrates β-hydroxybutyrate and acetoacetate with or without coenzyme gave little or no protection. However, 2-methyl malonate, a competitive inhibitor for β-hydroxybutyrate, strongly protected against inactivation. These studies indicate that: (1) a single arginine serves a vital role and is essential for function; (2) the arginine is located in the proximity of the substrate binding site." @default.
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- W2063735296 date "1983-11-01" @default.
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- W2063735296 title "Modification of arginines in d-β-hydroxybutyrate dehydrogenase" @default.
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- W2063735296 doi "https://doi.org/10.1016/0167-4838(83)90143-7" @default.
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