Fujita H, Ishida N, Akagi R
Department of Applied Physiology and Molecular Biology, Tohoku University School of Medicine.
Nihon Rinsho. 1995 Jun;53(6):1408-17.
delta-Aminolevulinate dehydratase (ALAD: E. C. 4.2.1.24), the second enzyme in the heme biosynthetic pathway, condenses two moles of delta-aminolevulinic acid to form porphobilinogen. ALAD deficiency is well known to develop signs and symptoms of typical hepatic porphyria, and classified into three categories as follows: (i) ALAD porphyria, a genetic defect of the enzyme, (ii) tyrosinemia type I, a genetic defect of fumarylacetoacetase in the tyrosine catabolic pathway, producing succinylacetone (a potent inhibitor of ALAD), and (iii) ALAD inhibition by environmental hazards, such as lead, trichloroethylene, and styrene. In the present article, we will describe molecular and biochemical mechanisms to cause the enzyme defect to discuss the significance of ALAD defect on human health.
δ-氨基乙酰丙酸脱水酶(ALAD:E.C.4.2.1.24)是血红素生物合成途径中的第二种酶,它将两摩尔的δ-氨基乙酰丙酸缩合形成胆色素原。众所周知,ALAD缺乏会引发典型肝卟啉症的体征和症状,并可分为以下三类:(i)ALAD卟啉症,该酶的一种遗传缺陷;(ii)I型酪氨酸血症,酪氨酸分解代谢途径中富马酰乙酰乙酸酶的一种遗传缺陷,会产生琥珀酰丙酮(一种强效的ALAD抑制剂);(iii)环境危害因素如铅、三氯乙烯和苯乙烯对ALAD的抑制作用。在本文中,我们将描述导致该酶缺陷的分子和生化机制,以探讨ALAD缺陷对人类健康的意义。