We are analyzing https://link.springer.com/article/10.1007/bf02110032.

Title:
Porphobilinogen synthase, the first source of Heme's asymmetry | Journal of Bioenergetics and Biomembranes
Description:
Porphobilinogen is the monopyrrole precursor of all biological tetrapyrroles. The biosynthesis of porphobilinogen involves the asymmetric condensation of two molecules of 5-aminolevulinate and is carried out by the enzyme porphobilinogen synthase (PBGS), also known as 5-aminolevulinate dehydratase. This review documents what is known about the mechanism of the PBGS-catalyzed reaction. The metal ion constitutents of PBGS are of particular interest because PBGS is a primary target for the environmental toxin lead. Mammalian PBGS contains two zinc ions at each active site. Bacterial and plant PBGS use a third metal ion, magnesium, as an allosteric activator. In addition, some bacterial and plant PBGS may use magnesium in place of one or both of the zinc ions of mammalian PBGS. These phylogenetic variations in metal ion usage are described along with a proposed rationale for the evolutionary divergence in metal ion usage. Finally, I describe what is known about the structure of PBGS, an enzyme which has as yet eluded crystal structure determination.
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Keywords {🔍}

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Topics {✒️}

month download article/chapter enzyme porphobilinogen synthase 5-aminolevulinate dehydratase privacy choices/manage cookies zinc phthalocyanines substituted asymmetric condensation related subjects full article pdf accession number u19876 accession number l31367 accession number x75043 european economic area environmental toxin lead porphobilinogen synthase sopena de kracoff conditions privacy policy metal ion constitutents nucleic acids res sequence analysis primer trace element res synthesis check access cancer research instant access metal ion usage accepting optional cookies ferramola de sancovich pbgs-catalyzed reaction sequence ofchlamydomonus pbgs journal finder publish main content log proteins 19 zinc ions innew comprehensive biochemistry enzyme inhib jaffe rights biosynthesis january 10 article jaffe article journal porphobilinogen involves porphobilinogen conundrum privacy policy 5-aminolevulinate personal data metal ion books a article log magnesium usage analysis

Schema {🗺️}

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         headline:Porphobilinogen synthase, the first source of Heme's asymmetry
         description:Porphobilinogen is the monopyrrole precursor of all biological tetrapyrroles. The biosynthesis of porphobilinogen involves the asymmetric condensation of two molecules of 5-aminolevulinate and is carried out by the enzyme porphobilinogen synthase (PBGS), also known as 5-aminolevulinate dehydratase. This review documents what is known about the mechanism of the PBGS-catalyzed reaction. The metal ion constitutents of PBGS are of particular interest because PBGS is a primary target for the environmental toxin lead. Mammalian PBGS contains two zinc ions at each active site. Bacterial and plant PBGS use a third metal ion, magnesium, as an allosteric activator. In addition, some bacterial and plant PBGS may use magnesium in place of one or both of the zinc ions of mammalian PBGS. These phylogenetic variations in metal ion usage are described along with a proposed rationale for the evolutionary divergence in metal ion usage. Finally, I describe what is known about the structure of PBGS, an enzyme which has as yet eluded crystal structure determination.
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            5-aminolevulinate dehydratase
            enzyme mechanisms
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            magnesium proteins
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            Animal Biochemistry
            Organic Chemistry
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      headline:Porphobilinogen synthase, the first source of Heme's asymmetry
      description:Porphobilinogen is the monopyrrole precursor of all biological tetrapyrroles. The biosynthesis of porphobilinogen involves the asymmetric condensation of two molecules of 5-aminolevulinate and is carried out by the enzyme porphobilinogen synthase (PBGS), also known as 5-aminolevulinate dehydratase. This review documents what is known about the mechanism of the PBGS-catalyzed reaction. The metal ion constitutents of PBGS are of particular interest because PBGS is a primary target for the environmental toxin lead. Mammalian PBGS contains two zinc ions at each active site. Bacterial and plant PBGS use a third metal ion, magnesium, as an allosteric activator. In addition, some bacterial and plant PBGS may use magnesium in place of one or both of the zinc ions of mammalian PBGS. These phylogenetic variations in metal ion usage are described along with a proposed rationale for the evolutionary divergence in metal ion usage. Finally, I describe what is known about the structure of PBGS, an enzyme which has as yet eluded crystal structure determination.
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      dateModified:
      pageStart:169
      pageEnd:179
      sameAs:https://doi.org/10.1007/BF02110032
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         Porphobilinogen synthase
         5-aminolevulinate dehydratase
         enzyme mechanisms
         zinc metalloenzyme
         magnesium proteins
         Bioorganic Chemistry
         Biochemistry
         general
         Animal Anatomy / Morphology / Histology
         Animal Biochemistry
         Organic Chemistry
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