May 1, 1976

Stability of some pyridoxal phosphate-dependent enzymes in vitamin B-6 deficient rats

The Journal of Nutrition
J E Hunter, A E Harper

Abstract

The effects of lowering the liver pyridoxal phosphate (PLP) concentration by vitamin B-6 deficiency on the stability of several rat liver enzymes were examined. Three PLP-dependent enzymes (serine dehydratase, ornithine-delta-aminotransferase, and tyrosine aminotransferase) and two non-PLP-dependent enzymes (glucose-6-phosphate dehydrogenase and phosphoenolpyruvate carboxykinase) were induced in vitamin B-6 deficient and control rats by feeding them high-protein diets or by injecting them with glucagon or dexamethasone. The decline of each activity was followed after withdrawal of the inducer. Serine dehydratase activity declined more rapidly in vitamin B-6 deficient than in control liver; however, ornithine aminotransferase and tyrosine aminotransferase activities were equally stable in deficient and control liver. Ornithine aminotransferase was predominantly in holoenzyme form in both control and deficient rats, whereas tyrosine aminotransferase was predominantly in apoenzyme form in both groups. The proportion of serine dehydratase in apoenzyme was less stable than the holoenzyme. Activity changes of glucose-6-phosphate dehydrogenase and phosphoenolpyruvate carboxykinase in control and vitamin B-6 deficient rats were similar...Continue Reading

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Mentioned in this Paper

Apoenzymes
Ornithine-oxo-acid aminotransferase
Desmolases
Tyrosine Aminotransferase
Oat
Pyridoxal Phosphate
Glucosephosphate Dehydrogenase
Transaminases
GTP-Dependent Phosphoenolpyruvate Carboxykinase
L-Serine Dehydratase

About this Paper

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