|
|
|
|
| LEADER |
01000caa a22002652c 4500 |
| 001 |
NLM275696987 |
| 003 |
DE-627 |
| 005 |
20250222070404.0 |
| 007 |
cr uuu---uuuuu |
| 008 |
231225s2017 xx |||||o 00| ||eng c |
| 024 |
7 |
|
|a 10.1016/j.plaphy.2017.08.030
|2 doi
|
| 028 |
5 |
2 |
|a pubmed25n0918.xml
|
| 035 |
|
|
|a (DE-627)NLM275696987
|
| 035 |
|
|
|a (NLM)28898745
|
| 035 |
|
|
|a (PII)S0981-9428(17)30286-3
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Méndez-Yañez, Ángela
|e verfasserin
|4 aut
|
| 245 |
1 |
0 |
|a Glycosylation is important for FcXTH1 activity as judged by its structural and biochemical characterization
|
| 264 |
|
1 |
|c 2017
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ƒaComputermedien
|b c
|2 rdamedia
|
| 338 |
|
|
|a ƒa Online-Ressource
|b cr
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 26.12.2017
|
| 500 |
|
|
|a Date Revised 30.09.2020
|
| 500 |
|
|
|a published: Print-Electronic
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a Copyright © 2017 Elsevier Masson SAS. All rights reserved.
|
| 520 |
|
|
|a Xyloglucan endotransglycosylase/hydrolases (XTH) may have endotransglycosylase (XET) and/or hydrolase (XEH) activities. Previous studies suggest that XTHs might play a key role in ripening of Fragaria chiloensis fruit as FcXTH1 transcripts increase as fruit softens. FcXTH1 protein sequence contains a conserved N-glycosylation site adjacent to catalytic residues. The FcXTH1 structure was built through comparative modeling methodology, the structure displays a β-jellyroll-type folding with a curvature generated by eight antiparallel β-sheets that holds the catalytic motif that is oriented towards the central cavity of the protein. Through Molecular Dynamic Simulations (MDS) analyses the protein-ligand interactions of FcXTH1 were explored, finding a better interaction with xyloglucans than cellulose. Nevertheless, the stability of the protein-ligand complex depends on the glycosylation state of FcXTH1: better energy interactions were determined for the glycosylated protein. As a complement, the molecular cloning and heterologous expression of FcXTH1 in Pichia pastoris was performed, and the recombinant protein was active and displayed strict XET activity. A KM value of 17.0 μM was determined for xyloglucan oligomer. The deglycosylation of FcXTH1 by PNGase-F treatment affects its biochemical properties (increase KM and reduce kcat/KM ratio) and reduces its stability. As a conclusion, glycosylation of FcXTH1 is important for its biological function
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a Cell wall disassembly
|
| 650 |
|
4 |
|a Fragaria chiloensis
|
| 650 |
|
4 |
|a Kinetic studies
|
| 650 |
|
4 |
|a Molecular modeling
|
| 650 |
|
4 |
|a N-protein glycosylation
|
| 650 |
|
4 |
|a Xyloglucan endotransglycosylase/hydrolases
|
| 650 |
|
7 |
|a Plant Proteins
|2 NLM
|
| 650 |
|
7 |
|a Glycosyltransferases
|2 NLM
|
| 650 |
|
7 |
|a EC 2.4.-
|2 NLM
|
| 650 |
|
7 |
|a xyloglucan - xyloglucosyltransferase
|2 NLM
|
| 650 |
|
7 |
|a EC 2.4.1.207
|2 NLM
|
| 700 |
1 |
|
|a Beltrán, Dina
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Campano-Romero, Constanza
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Molinett, Sebastián
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Herrera, Raúl
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Moya-León, María Alejandra
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Morales-Quintana, Luis
|e verfasserin
|4 aut
|
| 773 |
0 |
8 |
|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 119(2017) vom: 01. Okt., Seite 200-210
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnas
|
| 773 |
1 |
8 |
|g volume:119
|g year:2017
|g day:01
|g month:10
|g pages:200-210
|
| 856 |
4 |
0 |
|u http://dx.doi.org/10.1016/j.plaphy.2017.08.030
|3 Volltext
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_350
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 119
|j 2017
|b 01
|c 10
|h 200-210
|