Whiteman P A, Abraham E P
The Sir William Dunn School of Pathology, Oxford, UK.
FEBS Lett. 1996 Sep 23;394(1):31-3. doi: 10.1016/0014-5793(96)00925-8.
A phenoxymethylpenicillin amidohydrolase which hydrolyses phenoxymethylpenicillin to 6-aminopenicillanic acid (6-APA) has been isolated from two species of Penicillium chrysogenum. The amidohydrolase had a molecular mass of approx. 42 kDa. Its activity with benzylpenicillin as substrate was only 1.5% of that with phenoxymethylpenicillin and it was inhibited by its products. No penicillin formation from 6-APA and phenoxyacetyl or phenylacetyl coenzyme A was observed. The enzyme is thus distinct from the phenylacetyl coenzyme A:6-APA acyltransferase, which also has amidohydrolase activity and is involved in the final stages of the biosynthesis of penicillins.
已从两种产黄青霉中分离出一种苯氧甲基青霉素酰胺水解酶，该酶可将苯氧甲基青霉素水解为6-氨基青霉烷酸（6-APA）。该酰胺水解酶的分子量约为42 kDa。以苄青霉素为底物时，其活性仅为以苯氧甲基青霉素为底物时的1.5%，且会受到其产物的抑制。未观察到6-APA与苯氧乙酰辅酶A或苯乙酰辅酶A形成青霉素。因此，该酶与苯乙酰辅酶A：6-APA酰基转移酶不同，后者也具有酰胺水解酶活性，且参与青霉素生物合成的最后阶段。
