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PMID: 2494989 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The interaction of xylosyltransferase and glucuronyltransferase involved in glucuronoxylan synthesis in pea (Pisum sativum) epicotyls.

The Biochemical journal ·Vol. 257 ·No. 3 ·1989-02-01 ·Pages 853-8

Baydoun EA, Waldron KW, Brett CT

Abstract

A particulate enzyme preparation from etiolated pea (Pisum sativum) epicotyls was found to incorporate xylose from UDP-D-xylose into beta-(1----4)-xylan. The ability of this xylan to act as an acceptor for incorporation of [14C]glucuronic acid from UDP-D-[14C]glucuronic acid in a subsequent incubation was very limited, even though glucuronic acid incorporation was greatly prolonged when UDP-D-xylose was present in the same incubation as UDP-D-[14C]glucuronic acid. This indicated that glucuronic acid could not be added to preformed xylan. However, the presence of UDP-D-glucuronic acid inhibited incorporation of [14C]xylose from UDP-D-[14C]xylose into beta-(1----4)-xylan, and neither S-adenosylmethionine nor acetyl-CoA stimulated either the xylosyltransferase or the glucuronyltransferase.

MeSH Terms
Acetyl Coenzyme A/pharmacology Glucuronates/metabolism Glucuronic Acid Glucuronosyltransferase/metabolism Pentosyltransferases/metabolism Plants/enzymology,metabolism Polysaccharides/biosynthesis S-Adenosylmethionine/pharmacology Xylans/biosynthesis Xylose/metabolism
Chemicals
Glucuronates Polysaccharides Xylans glucuronoxylan Acetyl Coenzyme A S-Adenosylmethionine Glucuronic Acid Xylose Glucuronosyltransferase Pentosyltransferases UDP xylose-protein xylosyltransferase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Baydoun E A
Department of Biology, American University of Beirut, Lebanon.
Waldron K W
Brett C T
References (12)
12 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2570853
Published
1989-02-01
Pages
853-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1135666
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2570853 PMC Full Text View journal details
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