A novel galacturonide from Xanthomonas campestris

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Enzyme preparations from Xanthomonas campestris incubated in the presence of UDP-[14C]GlcA and Mg2+ produced a lipophilic galacturonide with unusual properties. It was easily degraded by both mild acid treatment (0.01 M-HCl, 100°C, 10 min) and mild alkali treatment (0.06 M-NaOH, room...

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Autores principales:	Baldessari, A., Ielpi, L., Dankert, M.A.
Formato:	Artículo publishedVersion
Publicado:	1990
Materias:	polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas campestris
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00221287_v136_n8_p1501_Baldessari https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00221287_v136_n8_p1501_Baldessari_oai
Aporte de:	Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires

id	I28-R145-paper_00221287_v136_n8_p1501_Baldessari_oai
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spelling	I28-R145-paper_00221287_v136_n8_p1501_Baldessari_oai2024-08-16 Baldessari, A. Ielpi, L. Dankert, M.A. 1990 Enzyme preparations from Xanthomonas campestris incubated in the presence of UDP-[14C]GlcA and Mg2+ produced a lipophilic galacturonide with unusual properties. It was easily degraded by both mild acid treatment (0.01 M-HCl, 100°C, 10 min) and mild alkali treatment (0.06 M-NaOH, room temperature, 5 min) releasing free [14C]galacturonic acid. The galacturonide appeared to be a single compound with one negative charge, as judged by TLC, paper electrophoresis and chromotography, LH-20 gel filtration and DEAE-cellulose column chromatography. Competition experiments indicated that the true glycosyl donor was UDP-GalA, in agreement with the detection of UDP-GlcA-4-epimerase activity in the crude enzyme preparation. The transglycosidase activity was located mainly in the membrane fraction. UDP inhibited the reaction and even produced some loss of label, suggesting an easily reversible reaction. UMP had almost no effect. Fil:Baldessari, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ielpi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Dankert, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. application/pdf http://hdl.handle.net/20.500.12110/paper_00221287_v136_n8_p1501_Baldessari info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar J. GEN. MICROBIOL. 1990;136(8):1501-1507 polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas Xanthomonas campestris A novel galacturonide from Xanthomonas campestris info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00221287_v136_n8_p1501_Baldessari_oai
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-145
collection	Repositorio Digital de la Universidad de Buenos Aires (UBA)
topic	polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas Xanthomonas campestris
spellingShingle	polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas Xanthomonas campestris Baldessari, A. Ielpi, L. Dankert, M.A. A novel galacturonide from Xanthomonas campestris
topic_facet	polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas Xanthomonas campestris
description	Enzyme preparations from Xanthomonas campestris incubated in the presence of UDP-[14C]GlcA and Mg2+ produced a lipophilic galacturonide with unusual properties. It was easily degraded by both mild acid treatment (0.01 M-HCl, 100°C, 10 min) and mild alkali treatment (0.06 M-NaOH, room temperature, 5 min) releasing free [14C]galacturonic acid. The galacturonide appeared to be a single compound with one negative charge, as judged by TLC, paper electrophoresis and chromotography, LH-20 gel filtration and DEAE-cellulose column chromatography. Competition experiments indicated that the true glycosyl donor was UDP-GalA, in agreement with the detection of UDP-GlcA-4-epimerase activity in the crude enzyme preparation. The transglycosidase activity was located mainly in the membrane fraction. UDP inhibited the reaction and even produced some loss of label, suggesting an easily reversible reaction. UMP had almost no effect.
format	Artículo Artículo publishedVersion
author	Baldessari, A. Ielpi, L. Dankert, M.A.
author_facet	Baldessari, A. Ielpi, L. Dankert, M.A.
author_sort	Baldessari, A.
title	A novel galacturonide from Xanthomonas campestris
title_short	A novel galacturonide from Xanthomonas campestris
title_full	A novel galacturonide from Xanthomonas campestris
title_fullStr	A novel galacturonide from Xanthomonas campestris
title_full_unstemmed	A novel galacturonide from Xanthomonas campestris
title_sort	novel galacturonide from xanthomonas campestris
publishDate	1990
url	http://hdl.handle.net/20.500.12110/paper_00221287_v136_n8_p1501_Baldessari https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00221287_v136_n8_p1501_Baldessari_oai
work_keys_str_mv	AT baldessaria anovelgalacturonidefromxanthomonascampestris AT ielpil anovelgalacturonidefromxanthomonascampestris AT dankertma anovelgalacturonidefromxanthomonascampestris AT baldessaria novelgalacturonidefromxanthomonascampestris AT ielpil novelgalacturonidefromxanthomonascampestris AT dankertma novelgalacturonidefromxanthomonascampestris
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A novel galacturonide from Xanthomonas campestris

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