Studies on the active sites and mechanisms of aspartate transaminase and malate dehydrogenase
Difluoro-oxaloacetate reacts with the aminic form of aspartate transaminase, forming a tight reversible complex as shown in steady state inhibition studies. Spectrophotmetric evidence indicates slow transamination of the analogue and allowed tentative identification of some of the reaction intermedi...
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University of Bath
1978
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| Online Access: | https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.473129 |