Tetrahedron Letters p. 5227 - 5230 (1999)
Update date:2022-08-28
Topics:
Shibasaki, Takeahi
Sakurai, Wataru
Hasegawa, Atsuhiro
Uosaki, Youichi
Mori, Hideo
Yoshida, Mayumi
Ozaki, Akio
Substrate selectivities of microbial proline 4-hydroxylase and proline 3-hydroxylases, all of which were purified from recombinant Escherichia coli, were investigated. L-2-Azetidine carboxylate, 3,4-dehydro-L-proline and L- pipecolinic acid were hydroxylated by those enzymes in regio- and stereospecific manner.
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