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

J.E. Baldwin; R.A. Field; C.C. Lawrence; V. Lee; J.K. Robinson; C.J. Schofield

doi:10.1016/S0040-4039(00)60753-0

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

J.E. Baldwin
, R.A. Field
, C.C. Lawrence
, V. Lee
, J.K. Robinson
, C.J. Schofield

Manchester Institute of Biotechnology

Research output: Contribution to journal › Article › peer-review

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.

Original language	Undefined
Pages (from-to)	4649-4652
Number of pages	4
Journal	Tetrahedron Letters
Volume	35
Issue number	26
DOIs	https://doi.org/10.1016/S0040-4039(00)60753-0
Publication status	Published - 9 Mar 1994

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Manchester Institute of Biotechnology

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10.1016/S0040-4039(00)60753-0

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

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.",

author = "J.E. Baldwin and R.A. Field and C.C. Lawrence and V. Lee and J.K. Robinson and C.J. Schofield",

year = "1994",

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doi = "10.1016/S0040-4039(00)60753-0",

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T1 - Substrate specificity of proline-4-hydroxylase: Chemical and enzymatic synthesis of 2S,3R,4S-epoxyproline

AU - Baldwin, J.E.

AU - Field, R.A.

AU - Lawrence, C.C.

AU - Lee, V.

AU - Robinson, J.K.

AU - Schofield, C.J.

PY - 1994/3/9

Y1 - 1994/3/9

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0028332587

U2 - 10.1016/S0040-4039(00)60753-0

DO - 10.1016/S0040-4039(00)60753-0

M3 - Article

SN - 0040-4039

VL - 35

SP - 4649

EP - 4652

JO - Tetrahedron Letters

JF - Tetrahedron Letters

IS - 26

ER -

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

Abstract

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