M. Kalinowska, GLUCOSYLATION OF C-19-HYDROXYSTEROID AND C-21-HYDROXYSTEROID BY SOLUBLE AND MEMBRANE-BOUND GLUCOSYLTRANSFERASE FROM OAT (AVENA-SATIVA) SEEDLINGS, Phytochemistry, 36(3), 1994, pp. 617-622
Several 3 beta-hydroxy derivatives of pregnane or androstane, containi
ng a planar ring system (5 alpha-H or Delta(5)), e.g. pregnenolone, ep
iandrosterone and dehydroisoandrosterone, are readily glucosylated by
delipidated enzyme preparations from oat seedlings in the presence of
UDPGlc. Two different glucosyl transferases are involved in these reac
tions: a soluble (cytosolic) enzyme with M(r) ca 65 000 and a membrane
-bound enzyme with M(r) ca 165 000. Both the cytosolic and membrane bo
und enzyme are present in green or etiolated leaves while roots contai
n only the membrane enzyme. Many properties of these two enzymes are v
ery similar to those of the cytosolic UDPGlc:nuatigenin glucosyltransf
erase and membrane bound UDPGlc:sterol glucosyltransferase, which were
detected previously in leaves of oat seedlings. The present results s
trongly suggest that the ability to glucosylate the pregnane or andros
tane derivatives by enzyme preparations from oat seedlings may be due
to relatively low substrate specificity of both UDPGlc:nuatigenin and
UDPGlc:sterol glucosyltransferase.