TY - JOUR
T1 - Substrate specificity of proline-4-hydroxylase
T2 - Chemical and enzymatic synthesis of 2S,3R,4S-epoxyproline
AU - Baldwin, Jack E.
AU - Field, Robert A.
AU - Lawrence, Christopher C.
AU - Lee, Victor
AU - Robinson, J. Kenneth
AU - Schofield, Christopher J.
PY - 1994/6/27
Y1 - 1994/6/27
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 - http://www.scopus.com/inward/record.url?scp=0028332587&partnerID=8YFLogxK
U2 - 10.1016/S0040-4039(00)60753-0
DO - 10.1016/S0040-4039(00)60753-0
M3 - Article
AN - SCOPUS:0028332587
VL - 35
SP - 4649
EP - 4652
JO - Tetrahedron Letters
JF - Tetrahedron Letters
SN - 0040-4039
IS - 26
ER -