Substrate specificity of a glucosyltransferase and an N-hydroxylase involved in the biosynthesis of cyclic hydroxamic acids in gramineae
dc.creator | Leighton, Victoria | |
dc.creator | Niemeyer, Hermann M. | |
dc.creator | Jonsson, Lisbeth M.V. | |
dc.date.accessioned | 2018-12-20T14:34:24Z | |
dc.date.available | 2018-12-20T14:34:24Z | |
dc.date.created | 2018-12-20T14:34:24Z | |
dc.date.issued | 1994 | |
dc.identifier | Phytochemistry, Volumen 36, Issue 4, 2018, Pages 887-892 | |
dc.identifier | 00319422 | |
dc.identifier | 10.1016/S0031-9422(00)90457-6 | |
dc.identifier | https://repositorio.uchile.cl/handle/2250/156530 | |
dc.description.abstract | Microsomal preparations from maize seedlings exhibited N-hydroxylase activity with 2-hydroxy-1,4-benzoxazin-3-one (HBOA) as substrate, but not with its 7-methoxy analogue (HMBOA), or their corresponding 2-O-β-d-glucosides. Extracts of the hydroxamic acid (Hx)-accumulating species rye, wheat and Hordeum lechleri, showed UDP-glucose:Hx-glucosyltransferase activity. The hydroxamic acid, 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA), and its 7-methoxy analogue, DIMBOA, were accepted as substrates, but not HBOA or HMBOA. The Hx-glucosyltransferase in the protein precipitate obtained between 30 and 60% ammonium sulphate saturation from either rye, wheat or H. lechleri had a higher Vmax value and lower Km value with DIMBOA as substrate. The Hx-glucosyltransferase from rye, which occurred in both roots and shoots throughout plant development, was purified 35-fold and characterized. The Mr of the enzyme was 43 000 and the isoelectric point 4.4. The Km values for DIBOA and DIMBOA in the partly puri | |
dc.language | en | |
dc.rights | http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Chile | |
dc.source | Phytochemistry | |
dc.subject | 1,4-benzoxazin-3-ones | |
dc.subject | DIBOA | |
dc.subject | DIMBOA | |
dc.subject | glucosyltransferase | |
dc.subject | Gramineae | |
dc.subject | HBOA | |
dc.subject | HMBOA. | |
dc.subject | hydroxamic acids | |
dc.subject | N-hydroxylase | |
dc.title | Substrate specificity of a glucosyltransferase and an N-hydroxylase involved in the biosynthesis of cyclic hydroxamic acids in gramineae | |
dc.type | Artículo de revista |