Biosynthesis of Tetrapyrroles by P.M. Jordan (Eds.)

By P.M. Jordan (Eds.)

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5) The transformation of the intermediate into uroporphyrinogen I11 does not require the participation of porphobilinogen deaminase or additional porphobilinogen units. 6) The two enzymes function independently and sequentially in the overall transformation of porphobilinogen into uroporphyrinogen 111. These enzymic experiments thus firmly established the transient species as the substrate for the uroporphyrinogen I11 synthase [222] and at a stroke eliminated virtually all previous mechanistic postulates.

5 sec-’ for the tetrapolymerization of porphobilinogen. 4. 75) have been isolated in homogeneous form due to their extreme instability and the lack, until recently, of a convenient assay method. c) purification methods and the development by Jordan of a rapid assay method for the enzyme [201]. The uroporphyrinogen synthases have been isolated in homogeneous form from human erythrocytes [202] and from a genetically engineered strain of E. cofi [203,204]. The enzyme has also been obtained in high purity from spinach [193], rat liver [205,206] and E.

These mechanistic details are included in Scheme 8. 8. Catalytic groups and the nature of the active site The enzyme groups responsible for catalysis have not been identified with any certainty with the exception of the active site lysine [169] K-252 in the human and rat A site P Site Aslte Psite Aslte Psite NHz A site P Site Asite Psite A site Scheme 8. Mechanism for 5-aminolaevulinicacid dehydratase P site A site P site 29 enzymes and K-258 in the E. colienzyme. The involvement of cysteine residues in the enzyme mechanism has been suggested from inactivation studies with iodoacetic acid and iodoacetamide which modify two highly reactive groups [148].

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