WebFeb 1, 2001 · Human porphobilinogen deaminase (PBGD) is, reportedly, encoded by 2 distinct messenger RNAs (mRNAs) transcribing from a single gene. The ubiquitous form …
Porphobilinogen deaminase - Wikipedia
WebThe three-dimensional structures of mutants of porphobilinogen deaminase: Toward an understanding of the structural basis of acute intermittent porphyria. Protein Science 1994, 3 (10) , 1644-1650. WebFeb 1, 2001 · Human porphobilinogen deaminase (PBGD) is, reportedly, encoded by 2 distinct messenger RNAs (mRNAs) transcribing from a single gene. The ubiquitous form of the PBGD gene product is often used as an endogenous reference in gene expression studies because it is pseudogene free and has minimal transcriptional variability among … open banking south africa
Structural basis of pyrrole polymerization in human porphobilinogen …
WebHuman porphobilinogen deaminase possess type 2 periplasmic binding protein fold Hydroxymethylbilane synthase (HMBS), also known as porphobilinogen deaminase … The structure of 40-42 kDa porphobilinogen deaminase, which is highly conserved amongst organisms, consists of three domains. Domains 1 and 2 are structurally very similar: each consisting of five beta-sheets and three alpha helices in humans. Domain 3 is positioned between the other two and has a flattened … See more Porphobilinogen deaminase (hydroxymethylbilane synthase, or uroporphyrinogen I synthase) is an enzyme (EC 2.5.1.61) that in humans is encoded by the HMBS gene. Porphobilinogen deaminase is … See more Functionally, porphobilinogen deaminase catalyzes the loss of ammonia from the porphobilinogen monomer (deamination) and its subsequent polymerization to a linear tetrapyrrole, … See more The most well-known health issue involving porphobilinogen deaminase is acute intermittent porphyria, an autosomal dominant genetic … See more • GeneReviews/NCBI/NIH/UW entry on Hydroxymethylbilane Synthase Deficiency • Overview of all the structural information available in the See more The first step is believed to involve an E1 elimination of ammonia from porphobilinogen, generating a carbocation intermediate (1). This intermediate is then attacked by the … See more • Deybach JC, Puy H (1995). "Porphobilinogen deaminase gene structure and molecular defects". J. Bioenerg. … See more WebFunction. Porphobilinogen deaminase (PBGD) also known as Hydroxymethylbilane synthase, is a monomeric deaminase and is the third enzyme in the heme biosynthesis pathways in mammals [1]. It catalyses the polymerization of four porphobilinogen molecules to yield hydroxymethylbilane, a precursor in the formation of Porphyrin [2]. open banking republic of ireland