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By P.M. Jordan (Eds.)

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Such ring opening (mutarotation) occurs routinely in enzymic transformations involving glucose and other sugars. Most recently the aminotransferase cDNA has been isolated from barley [ 1261and the derived protein sequence has been shown to be similar to that of Salmonella typhimurium [104]. The aminotransferase reaction in which glutamate 1-semialdehyde is transformed into 5-aminolaevulinic acid by a single enzyme, glutamate 1-semialdehyde aminotransferase has been challenged by Dornemann [127] as a result of experiments carried out with Scenedesmus.

These findings suggest that either zinc and lead may interact with the human enzyme at more than one site [165] or that half site reactivity is involved. Alternatively a regulatory mechanism may be involved in which the binding of lead to four of the subunits in the octamer may induce a conformational change in the other four subunits which results in the total loss of activity. The EXAFS data discussed above [159] may be consistent with these observations. 6. Nature of the uctive site groups The first detailed studies on the mechanism of action of 5-aminolaevulinic acid dehydratase were those carried out by Shemin and his colleagues with the enzyme from R.

The aminotransferase appears to function without the necessity for any amino acid amino-donor such as glutamate and the substrate itself supplies the amino group. The mechanism has been studied using glutamate doubly labelled with l3C,’’Nby Mau and Wang [125] who have suggested that intermolecular transfer of the amino group takes place. These results, however, need to be interpreted with caution because of the possibility of exchange. One of the most interesting properties of the aminotransferase is its remarkable sensitivity to gabaculine [ 1221 suggesting that pyridoxal 5’-phosphate is involved in the enzyme reaction.

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