Some research results on rice and Arabidopsis thaliana found that the formation of chlorophyll-deficient mutant was the block of chlorophyll biosynthesis regulated by enzymes of D-aminolevulinate dehydratase (ALAD), porphobilinogen deaminase
(PBGD) and magnesium chelatase (Mg-chelatase) (Rissler et al., 2002; Xu et al., 2006; Wu et al., 2007; Zong et al., 2013).
Acute intermittent porphyria in Sweden: Molecular, functional and clinical consequences of some new mutations found in the porphobilinogen deaminase
Porphyria is a group of disorders caused by the accumulation of porphyrin and porphyrin precursors due to the abnormalities in certain enzymes that normally participate in the production of haem.1 Acute intermittent porphyria (AIP), an autosomal dominant disorder, is a common type of neurologic porphyria in which mutation of the porphobilinogen deaminase
(PBGD) gene plays an important role.2,3 The clinical manifestations of AIP include severe abdominal pain, nausea, vomiting and psychiatric symptoms, but not skin lesions.4 Here, we report a case of AIP with mutant allele of the PBGD gene.
For confirmatory diagnosis, porphobilinogen deaminase
(PBGD) test was done which was found to be positive.
Acute intermittent porphyria (AIP) is the most common of the acute hepatic porphyrias, and results from partial deficiency of porphobilinogen deaminase
, the third enzyme of the haem synthetic pathway [Badminton and Elder, 2002].
Some research results on rice and Arabidopsis thaliana found that the formation of chlorophyll-deficient mutant was the block of chlorophyll biosynthesis regulated by enzymes of d- aminolevulinate dehydratase (ALAD), porphobilinogen deaminase
(PBGD) and magnesium chelatase (Mg- chelatase) (Rissler et al., 2002; Xu et al., 2006; Wu et al., 2007; Zong et al., 2013).
Alternative transcription and splicing of the human porphobilinogen deaminase
gene result either in tissue-specific or in housekeeping expression.
Allosteric inhibition of human lymphoblast and purified porphobilinogen deaminase
by protoporphyrinogen and coproporphyrinogen: a possible mechanism for the acute attack of variegate porphyria.
In distribution E, 13 of the 15 reported results were belowthe lower reference limits for porphobilinogen deaminase
(PBGD), and 2 of 4 for uroporphyrinogen decarboxylase (UROD).
In preliminary experiments, amplification factors were determined for specific target sequences Mus musculus glyceraldehyde-3-phosphate dehydrogenase gene 3' untranslated region (Gapd 3'-UTR), Gapd, and Mus musculus porphobilinogen deaminase
Acute intermittent porphyria (AIP) (4) is an autosomal dominant disorder caused by a metabolic error in heme biosynthesis in which the third enzyme, porphobilinogen deaminase
(PBGD; EC 220.127.116.11), also called hydroxymethylbilane synthase, is deficient.
Some consistency in enzyme nomenclature is called for; uroporphyrinogen I synthase and porphobilinogen deaminase
should be confined to the dust bin of history--hydroxymethyl bilane synthase is the correct and internationally preferred term.