Literature DB >> 7616655

[delta-Aminolevulinate dehydratase deficiency].

H Fujita1, N Ishida, R Akagi.   

Abstract

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.

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Year:  1995        PMID: 7616655

Source DB:  PubMed          Journal:  Nihon Rinsho        ISSN: 0047-1852


  1 in total

1.  ALAD porphyria is a conformational disease.

Authors:  Eileen K Jaffe; Linda Stith
Journal:  Am J Hum Genet       Date:  2006-12-21       Impact factor: 11.025

  1 in total

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