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dc.contributor.authorKaraman, Rafik
dc.date.accessioned2018-09-29T13:32:28Z
dc.date.available2018-09-29T13:32:28Z
dc.date.issued2012-11-16
dc.identifier.citationKaraman R (2013) Computationally Designed Enzyme Models to Replace Natural Enzymes in Prodrug Approaches. Drug Des 2: e111. doi:10.4172/2169- 0138.1000e111en_US
dc.identifier.issn2169-0138
dc.identifier.urihttps://dspace.alquds.edu/handle/20.500.12213/1021
dc.description.abstractThe striking efficiency of enzyme catalysis has inspired many organic chemists to explore enzyme mechanisms by studying certain intra molecular processes such as enzyme models which proceed faster than their intermolecular counterparts. This research brings about the important question of whether enzyme models will replace natural enzymes in the conversion of prodrugs to their parental drugs. Enzymes are mandatory for the inter conversion of many prodrugs to their parental drugs. Among the most important enzymes in the bioconversion of prodrugs are amides (ex. trypsin, chymotrypsin, elastase, carboxypeptidase, and aminopeptidase) and ester-based prodrugs (ex. paraoxonase, carboxylesterase, acetylcholinesterase and cholinesterase). Most of these enzymes are hydrolytic enzymes, however, non-hydrolytic enzymes, including all cytochrome P450 enzymes, are also capable of catalyzing the bioconversion of ester and amide-based prodrugs [1].en_US
dc.description.sponsorshipThe author would like to acknowledge funding by the German Research Foundation (DFG, ME 1024/8-1).en_US
dc.language.isoen_USen_US
dc.titleComputationally Designed Enzyme Models to Replace Natural Enzymes in Prodrug Approachesen_US
dc.typeArticleen_US


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