NDLI: Purification and Characterization of Enzymes Exhibiting β-d-Xylosidase Activities in Stem Tissues of Arabidopsis1

Content Provider	PubMed Central
Author	Minic, Zoran Christophe, Rihouey Do, Cao Trung Lerouge, Patrice Jouanin, Lise
Copyright Year	2004
Abstract	This work describes the purification and characterization of enzymes that exhibit β-d-xylosidase activity in stem tissues of Arabidopsis. This is the first detailed investigation that concerns the characterization of catalytic properties and sequence identity of enzymes with β-d-xylosidase activities in a dicotyledonous plant. Three different enzymes, ARAf, XYL4, and XYL1 with apparent molecular masses of 75, 67, and 64 kD, respectively, were purified to homogeneity. ARAf was identified as a putative α-l-arabinofuranosidase, and XYL4 and XYL1 as putative β-d-xylosidases using matrix-assisted laser-desorption ionization time of flight. ARAf belongs to family 51 and XYL4 and XYL1 to family 3 of glycoside hydrolases. ARAf and XYL1 have highest specificity for p-nitrophenyl-α-l-arabinofuranoside and XYL4 for p-nitrophenyl-β-d-xylopyranoside and natural substrates such as xylobiose and xylotetraose. XYL4 was shown to release mainly d-Xyl from oat spelt xylan, rye arabinoxylan, wheat arabinoxylan, and oligoarabinoxylans. ARAf and XYL1 can also release d-Xyl from these substrates but less efficiently than XYL4. Moreover, they can also release l-Ara from arabinoxylans and arabinan. Overall, the results indicate that XYL4 possesses enzymatic specificity characteristic for a β-d-xylosidase, while ARAf and XYL1 act as bifunctional α-l-arabinofuranosidase/β-d-xylosidases. Analysis of the activity of these three enzymes in stem tissues at different stages of development has shown that young stems possess the highest activities for all three enzymes in comparison to the activities of the enzymes present in stems at older stages of development. High enzyme activities are most likely related to the necessary modifications of cell wall structure occurring during plant growth.
Related Links	http://dx.doi.org/10.1104/pp.104.041269
Starting Page	867
File Format	PDF
ISSN	15322548
e-ISSN	15322548
Journal	Plant Physiology
Issue Number	2
Volume Number	135
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2004-06-01
Access Restriction	Open
Rights Holder	American Society of Plant Biologists
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics Physiology Plant Science

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1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
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