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- W86553572 abstract "5-Aminolevulinic acid dehydratase (ALAD, 5-aminolevulinate hydrolyase, EC 4.2.1.24) catalyzes the synthesis of the pyrrole porphobilinogen from 2 molecules of 5- aminolevulinic acid. The enzyme from bovine liver has a molecular weight of 280.000 daltons and consists of eight subunits of 35.000 daltons each [1]. Lysine, hystidine and cysteine have been identified as amino acid constituents of the enzyme protein involved in the active site [2]. Two cysteine residues essential for the enzyme activity are rapidly oxidized by air, and the maintenance of the active state requires the presence of a thiol [3]. The isolated enzyme protein contains 2–6 g. atoms of zinc per octamer and it binds a maximum number of eight zinc ions per octamer with high affinity [4]. The function of zinc in ALAD is not clear. Several findings imply a direct catalytic function for zinc whilst other results support the assumption that zinc stabilizes the active structure of the enzyme protein, without directly interacting with the substrate." @default.
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- W86553572 date "1984-01-01" @default.
- W86553572 modified "2023-09-24" @default.
- W86553572 title "EXAFS Investigations of Zinc in 5-Aminolevulinic Acid Dehydratase" @default.
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- W86553572 doi "https://doi.org/10.1007/978-3-642-46522-2_35" @default.
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