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  2. Porphyrin - Wikipedia

    en.wikipedia.org/wiki/Porphyrin

    The following scheme summarizes the biosynthesis of porphyrins, with references by EC number and the OMIM database. The porphyria associated with the deficiency of each enzyme is also shown: Heme B biosynthesis pathway and its modulators. Major enzyme deficiences are also shown.

  3. Porphobilinogen - Wikipedia

    en.wikipedia.org/wiki/Porphobilinogen

    In the typical porphyrin biosynthesis pathway, four molecules of porphobilinogen are concatenated by carbons 2 and 5 of the pyrrole ring (adjacent to the nitrogen atom) into hydroxymethyl bilane by the enzyme porphobilinogen deaminase, also known as hydroxymethylbilane synthase.

  4. Porphobilinogen deaminase - Wikipedia

    en.wikipedia.org/wiki/Porphobilinogen_deaminase

    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 involved in the third step of the heme biosynthetic pathway.

  5. Aminolevulinic acid synthase - Wikipedia

    en.wikipedia.org/wiki/Aminolevulinic_acid_synthase

    Other organisms produce ALA through a three enzyme pathway known as the C5 pathway. ALA is synthesized through the condensation of glycine and succinyl-CoA. In humans, transcription of ALA synthase is tightly controlled by the presence of Fe 2+-binding elements, to prevent accumulation of porphyrin intermediates in the absence of iron. There ...

  6. Protoporphyrin IX - Wikipedia

    en.wikipedia.org/wiki/Protoporphyrin_IX

    The last step is mediated by the enzyme protoporphyrinogen oxidase. Protoporphyrin IX is an important precursor to biologically essential prosthetic groups such as heme, cytochrome c, and chlorophylls. As a result, a number of organisms are able to synthesize this tetrapyrrole from basic precursors such as glycine and succinyl-CoA, or glutamic ...

  7. Acute intermittent porphyria - Wikipedia

    en.wikipedia.org/wiki/Acute_intermittent_porphyria

    Acute intermittent porphyria (AIP) is a rare metabolic disorder affecting the production of heme resulting from a deficiency of the enzyme porphobilinogen deaminase. It is the most common of the acute porphyrias. [1] [2] [3]

  8. Porphyria cutanea tarda - Wikipedia

    en.wikipedia.org/wiki/Porphyria_cutanea_tarda

    Porphyrins interact with iron, absorbing photons to create reactive oxygen species is the mechanism of action causing the itchy, painful blisters of PCT. [7] The reactive oxygen species consume the skin antioxidants beta-carotene, vitamin E, and vitamin C. Supplementation of these three vitamins reduces the oxidation and potentially diminishes ...

  9. Coproporphyrinogen III oxidase - Wikipedia

    en.wikipedia.org/wiki/Coproporphyrinogen_III_oxidase

    CPOX is an enzyme involved in the sixth step of porphyrin metabolism it catalyses the oxidative decarboxylation of coproporphyrinogen III to proto-porphyrinogen IX in the haem and chlorophyll biosynthetic pathways. [5] [11] The protein is a homodimer containing two internally bound iron atoms per molecule of native protein. [12]