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231225s2020 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2020.153210
|2 doi
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|a pubmed25n1037.xml
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|a (DE-627)NLM311236650
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|a (NLM)32544741
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|a (PII)S0176-1617(20)30100-0
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Holland, Claire
|e verfasserin
|4 aut
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|a Three highly acidic Equisetum XTHs differ from hetero-trans-β-glucanase in donor substrate specificity and are predominantly xyloglucan homo-transglucosylases
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|c 2020
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 08.12.2020
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|a Date Revised 14.12.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2020 Elsevier GmbH. All rights reserved.
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|a Transglycanases are enzymes that remodel the primary cell wall in plants, potentially loosening and/or strengthening it. Xyloglucan endotransglucosylase (XET; EC 2.4.1.207), ubiquitous in land plants, is a homo-transglucanase activity (donor, xyloglucan; acceptor, xyloglucan) exhibited by XTH (xyloglucan endotransglucosylase/hydrolase) proteins. By contrast, hetero-trans-β-glucanase (HTG) is the only known enzyme that is preferentially a hetero-transglucanase. Its two main hetero-transglucanase activities are MLG : xyloglucan endotransglucosylase (MXE) and cellulose : xyloglucan endotransglucosylase (CXE). HTG is highly acidic and found only in the evolutionarily isolated genus of fern-allies, Equisetum. We now report genes for three new highly acidic HTG-related XTHs in E. fluviatile (EfXTH-A, EfXTH-H and EfXTH-I). We expressed them heterologously in Pichia and tested the encoded proteins' enzymic activities to determine whether their acidity and/or their Equisetum-specific sequences might confer high hetero-transglucanase activity. Untransformed Pichia was found to secrete MLG-degrading enzyme(s), which had to be removed for reliable MXE assays. All three acidic EfXTHs exhibited very predominantly XET activity, although low but measurable hetero-transglucanase activities (MXE and CXE) were also detected in EfXTH-H and EfXTH-I. We conclude that the extremely high hetero-transglucanase activities of Equisetum HTG are not emulated by similarly acidic Equisetum XTHs that share up to 55.5% sequence identity with HTG
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|a Journal Article
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|a Cell elongation
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|a Equisetum
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|a Hetero-trans-β-glucanase
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|a Heterologous expression
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|a Pichia pastoris
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|a Plant cell wall
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|a Xyloglucan endotransglucosylase
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|a Plant Proteins
|2 NLM
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|a Glycosyltransferases
|2 NLM
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|a EC 2.4.-
|2 NLM
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|a xyloglucan - xyloglucosyltransferase
|2 NLM
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|a EC 2.4.1.207
|2 NLM
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|a Simmons, Thomas J
|e verfasserin
|4 aut
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|a Meulewaeter, Frank
|e verfasserin
|4 aut
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|a Hudson, Andrew
|e verfasserin
|4 aut
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|a Fry, Stephen C
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 251(2020) vom: 20. Aug., Seite 153210
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnas
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| 773 |
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|g volume:251
|g year:2020
|g day:20
|g month:08
|g pages:153210
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|u http://dx.doi.org/10.1016/j.jplph.2020.153210
|3 Volltext
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|d 251
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