BIOCHEMICAL-STUDIES ON THE ENZYMATIC DEFICIENCIES IN HEREDITARY TYROSINEMIA
BIOCHEMICAL-STUDIES ON THE ENZYMATIC DEFICIENCIES IN HEREDITARY TYROSINEMIA
复制标题
DOI:
10.1016/0009-8981(83)90191-2
复制
发表时间:
1983-01-01
影响因子:
5
通讯作者:
SMITH, GPA
中科院分区:
文献类型:
--
作者:
BERGER, R;VANFAASSEN, H;SMITH, GPA
Experiments are described on the effects of succinylacetone and fumarylacetoacetate on .delta.-aminolevulinic acid dehydratase, methionine adenosyltransferase and p-OH-phenylpyruvate dioxygenase. .delta.-Aminolevulinic acid dehydratase from human erythrocytes is inhibited non-competitively by succinylacetone (Ki 0.03 .mu.mol/l) and by fumarylacetoacetate (Ki 0.06 .mu.mol/l). The inhibition by succinylacetone is not prevented by dithiothreitol, but the inhibition by fumarylacetoacetate is not observed if dithiothreitol is present. Methionine adenosyltransferase, partially purified from rabbit liver, is not inhibited by succinylacetone but is inhibited by fumarylacetoacetate: 69% inhibition is observed at 1 mmol/l. Human liver p-OH-phenylpyruvate dioxygenase is not inhibited by succinylacetone or fumarylacetoacetate. Secondary enzyme deficiences observed in hereditary tyrosinemia (.delta.-aminolevulinic acid dehydratase, methionine adenosyltransferase) are the result of inhibition by succinylacetone and fumarylacetoacetate, accumulating as a result of a primary deficiency of fumarylacetoacetase.