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

1989 ◽  
Vol 257 (3) ◽  
pp. 853-858 ◽  
Author(s):  
E A H Baydoun ◽  
K W Waldron ◽  
C T Brett
Keyword(s):  
Pisum Sativum ◽  
Enzyme Preparation ◽  
Glucuronic Acid ◽  
Acetyl Coa ◽  
Acid Incorporation

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.

scholarly journals A glucuronyltransferase involved in glucuronoxylan synthesis in pea (Pisum sativum) epicotyls

1983 ◽  
Vol 213 (1) ◽  
pp. 115-122 ◽  
Author(s):  
K W Waldron ◽  
C T Brett
Keyword(s):  
Pisum Sativum ◽  
Acid Hydrolysis ◽  
Paper Chromatography ◽  
Enzyme Preparation ◽  
Glucuronic Acid ◽  
Optimum Conditions ◽  
Total Acid

A particulate enzyme preparation made from epicotyls of 1-week-old etiolated pea (Pisum sativum) seedlings was shown to incorporate glucuronic acid from UDP-D-[U-14C]glucuronic acid into a hemicellulosic polysaccharide. Optimum conditions for the incorporation include the presence of Mn2+ ions at between 4 and 10 mmol/litre and a pH between 5 and 6. UDP-D-xylose at 1 mmol/litre allows incorporation to continue for at least 8 h. In its absence, the reaction stops within 30 min. Analysis of the product by partial and total acid hydrolysis, followed by paper chromatography or electrophoresis, indicates that the polysaccharide produced is a glucuronoxylan.

scholarly journals Nuclear-Cytoplasmic Conflict in Pea (Pisum sativum L.) Is Associated with Nuclear and Plastidic Candidate Genes Encoding Acetyl-CoA Carboxylase Subunits

PLoS ONE ◽  
2015 ◽  
Vol 10 (3) ◽  
pp. e0119835 ◽  
Author(s):  
Vera S. Bogdanova ◽  
Olga O. Zaytseva ◽  
Anatoliy V. Mglinets ◽  
Natalia V. Shatskaya ◽  
Oleg E. Kosterin ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Candidate Genes ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Pisum Sativum L ◽  
Genes Encoding

Notes: Inhibition of the Acetyl-CoA Carboxylase of Barley Chloroplasts by Cycloxydim and Sethoxydim

1987 ◽  
Vol 42 (11-12) ◽  
pp. 1361-1363 ◽  
Author(s):  
Manfred Focke ◽  
Hartmut K. Lichtenthaler
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Enzyme Preparation ◽  
Fatty Acid Biosynthesis ◽  
De Novo ◽  
Acetyl Coa Carboxylase ◽  
Acid Biosynthesis ◽  
Hordeum Vulgare L ◽  
Acetyl Coa ◽  
Malonyl Coa

The effect of the three cyclohexane-1,3-dione derivatives cycloxydim, sethoxydim and clethodim on the incorpora­tion of 14C-labelled acetate, malonate. acctyl-CoA or malonyl-CoA into fatty acids was studied in an enzyme preparation isolated from barley chloroplasts (Hordeum vulgare L. var. “Alexis”). The herbicides cycloxydim, clethodim and sethoxydim block the de novo fatty acid biosynthesis from [2-14C]acetatc and [1-14C]acetyl-CoA, whereas that of [2-14C]malonatc and [2-14C)malonyl-CoA is not affected. The data indicate that the mode of action of the cyclohexane-1,3-dione derivatives in the sensitive bar­ley plant consists in the inhibition of de novo fatty acid biosynthesis by blocking the acetyl-CoA carboxylase (EC 6.4.1.2.).

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