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Science 6 February 1970:
Vol. 167. no. 3919, pp. 887 - 889
DOI: 10.1126/science.167.3919.887
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Articles

Substrate Stabilization: Genetically Controlled Reciprocal Relationship of Two Human Enzymes

Martin L. Greene 1, James A. Boyle 1, and J. Edwin Seegmiller 1

1 Section on Human Biochemical Genetics, National Institute of Arthritis and Metabolic Disease, Bethesda, Maryland 20014

5-Phosphoribosyl-l-pyrophosphate, a substrate shared by adenine phosphoribosyltransferase and hypoxanthine-guanine phosphoribosyltransferase, accumulates in human erythrocytes lacking hypoxanthine-guanine phosphoribosyltransferase. 5-Phosphoribosyl-l-pyrophosphate added to purified adenine phosphoribosyltransferase stabilizes it against heat inactivation. The increased activity of adenine phosphoribosyltransferase seen in erythrocytes deficient in hypoxanthine-guanine phosphoribosyltransferase may result from substrate stabilization of this enzyme in vivo.


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