Substrate specificity of proline-4-hydroxylase:Chemical and enzymatic synthesis of 2S,3R,4S-epoxyproline

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Baldwin, Jack E., Field, Robert A. ORCID: https://orcid.org/0000-0001-8574-0275, Lawrence, Christopher C., Lee, Victor, Robinson, J. Kenneth and Schofield, Christopher J. (1994) Substrate specificity of proline-4-hydroxylase:Chemical and enzymatic synthesis of 2S,3R,4S-epoxyproline. Tetrahedron Letters, 35 (26). pp. 4649-4652. ISSN 0040-4039

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Abstract

The substrate specificity of L-proline-4-hydroxylase, a 2-oxoglutarate dependent dioxygenase from Streptomyces griseoviridus P8648, was investigated. Preliminary assays measuring turnover of 2-oxoglutarate indicated 3,4-dehydro-L-proline was an efficient substrate. The identity of the product was shown to be 2S,3R,4S-epoxy-L-proline by comparison with synthetic 2S,3R,4S- and 2S,3S,4R-epoxy-L-prolines.

Item Type: Article
Uncontrolled Keywords: biochemistry,drug discovery,organic chemistry ,/dk/atira/pure/subjectarea/asjc/1300/1303
Faculty \ School: Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
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Depositing User: LivePure Connector
Date Deposited: 11 Sep 2024 14:30
Last Modified: 18 Jun 2026 20:21
URI: https://ueaeprints.uea.ac.uk/id/eprint/96719
DOI: 10.1016/S0040-4039(00)60753-0

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