Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.353938
Title: Mechanistic studies on enzyme-catalysed dimerization reactions
Author: Gibbs, Philip
ISNI:       0000 0001 3496 9133
Awarding Body: University of Southampton
Current Institution: University of Southampton
Date of Award: 1984
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Abstract:
5-Aminolevulinic acid dehydratase catalyses a dimerization reaction whereby the two identical substrate molecules, 5-aminolevulinic acid, are condensed together to yield porphobilinogen, the monopyrrolic precursor of porphyrin biosynthesis. A new procedure for the purification of the enzyme from human erythrocytes was developed and yielded 27.5 mg of pure enzyme protein in good recovery with a high specific activity (24.0 units/mg protein). The human enzyme was treated with [4-14c] aminolevulinic acid and the resulting Schiff base complex was reduced with sodium borohydride. The modified protein was cleaved with cyanogen bromide and the peptide containing the label was isolated and sequenced. Similar studied were performed on the enzyme isolated from bovine liver. Comparison of the two active site sequences revealed a common hexapeptide which had the following structure where X* is amino acid -4-14C 5-aminolevulinic acid adduct (probably ALA-lysine).
Supervisor: Jordan, Peter Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.353938  DOI: Not available
Keywords: Enzyme reactions
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