L-Threonine dehydrogenase from goat liver. Feedback inhibition by methylglyoxal.
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منابع مشابه
Rat liver L-threonine dehydrogenase.
L-threonine dehydrogenase (E.C.1.1.1.103) catalyzes the NAD+-dependent transformation of Lthreonine to 2-amino 3-0x0-butyric acid, which spontaneously loses CO2 with the final production of aminoacetone ( 1) The enzyme is present in several microorganisms as well as in the liver of vertebrates (2-6). We studied some properties of the rat liver enzyme, showing that the activity was strongly inhi...
متن کاملInhibition of succinic dehydrogenase by methylglyoxal.
The reaction of the carbonyl group of methylglyoxal with -SH radicals of thiols has been the subject of numerous investigations (l-9). The reactivity of the keto aldehyde with -SH compounds suggested that a similar type of reaction may occur between methylglyoxal and -SH proteins. The physiological r&e of methylglyoxal as an inhibitor of -SK enzymes is of particular interest, since this keto al...
متن کاملMetabolic homoeostasis of L-threonine in the normally-fed rat. Importance of liver threonine dehydrogenase activity.
Threonine dehydratase, threonine aldolase and threonine dehydrogenase activities were assayed in livers of rats that had been normally-fed, starved for 72 h, fed a high-protein diet or normally-fed and injected with glucagon or cortisone. A modified continuous spectrophotometric assay for threonine aldolase overcame interference resulting from threonine dehydratase activity and revealed that th...
متن کاملInhibition of Translation by Methylglyoxal
Methylglyoxal was a weak inhibitor of translation in the r e t i c u l o c y t e l y s a t e c e l l f r e e system and it did not display cap-dependent inhibition. A similar inhibition was obtained in a wheat-germ cei l f ree system that d i sp layed extensive cap-dependent inhibition with the cap ana logue 7 m e t h y J g u a n o s i n e phosphate . These results show that the chemical reacti...
متن کاملL-Threonine dehydrogenase of chicken liver. Purification, characterization, and physiological significance.
L-Threonine dehydrogenase (L-threonine:NAD+ oxidoreductase (EC 1.1.1.103) has been purified to apparent homogeneity from chicken liver mitochondria. The presence of 2-mercaptoethanol and glycerol is necessary for stabilizing the enzyme during purification and storage. The enzyme is a monomer and has Mr approximately equal to 88,000. The pH optimum is 8.6 to 8.7, and the isoelectric point of the...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)88915-3