Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Glycoside hydrolase Family 35"'
Publikováno v:
Plants
Volume 10
Issue 8
Plants, Vol 10, Iss 1639, p 1639 (2021)
Volume 10
Issue 8
Plants, Vol 10, Iss 1639, p 1639 (2021)
Plant β-galactosidases (BGAL) function in various cell wall biogeneses and modifications, and they belong to the glycoside hydrolase family. However, the roles of BGAL family members in Medicago
truncatula cell wall remodeling remain uncle
truncatula cell wall remodeling remain uncle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c23b49cbdf21625d4f0f7f8f73b4aa4c
https://doi.org/10.3390/plants10081639
https://doi.org/10.3390/plants10081639
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1864:1411-1418
Most plant β-galactosidases, which belong to glycoside hydrolase family 35, have a C-terminal domain homologous to animal galactose and rhamnose-binding lectins. To investigate the structure and function of this domain, the C-terminal domain of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d9f2f561cd5d5ef92eb59e8f941d751
https://doi.org/10.1016/j.bbapap.2016.07.005
https://doi.org/10.1016/j.bbapap.2016.07.005
Akademický článek
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Publikováno v:
FEBS Letters. 580:4377-4381
The identity of the acid/base catalyst of the Family 35 beta-galactosidases from Xanthomonas manihotis (BgaX) has been confirmed as Glu184 by kinetic analysis of mutants modified at that position. The Glu184Ala mutant of BgaX is shown to function as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a0264fd4f1762ecca6569eaf44bc53e
https://doi.org/10.1016/j.febslet.2006.06.095
https://doi.org/10.1016/j.febslet.2006.06.095
Autor:
M. Esperanza Cerdán, Mercedes Ramírez-Escudero, Julia Sanz-Aparicio, Agustín Rico-Díaz, Ángel Vizoso-Vázquez, Manuel Becerra
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
β-Galactosidases are biotechnologically interesting enzymes that catalyze the hydrolysis or transgalactosylation of β-galactosides. Among them, the Aspergillus niger β-galactosidase (AnβGal) belongs to the glycoside hydrolase family 35 (GH35) and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::381babf2069423258ff8a01f0276b81b
http://hdl.handle.net/10261/165815
http://hdl.handle.net/10261/165815
Publikováno v:
Applied Microbiology and Biotechnology. 97:2895-2906
An endo-β-1,4-galactanase (PcGAL1) and an exo-β-1,4-galactanase (PcGALX35C) were purified from the culture filtrate of Penicillium chrysogenum 31B. Pcgal1 and Pcgalx35C cDNAs encoding PcGAL1 and PcGALX35C were isolated by in vitro cloning. The dedu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0285d0be37d575c2eb94fe08f50a7f1c
https://doi.org/10.1007/s00253-012-4154-5
https://doi.org/10.1007/s00253-012-4154-5
Autor:
Jonathan E. Poulton, Ming-Che Shih, Hsiao Ping Peng, Joseph T. Miller, Chi-Lien Cheng, Meiying Zheng, Asim Esen, Shin-Han Shiu, Jonas Benson, Young Ock Ahn, David R. Bevan
Publikováno v:
Phytochemistry. 68:1510-1520
In plants, Glycoside Hydrolase (GH) Family 1 β-glycosidases are believed to play important roles in many diverse processes including chemical defense against herbivory, lignification, hydrolysis of cell wall-derived oligosaccharides during germinati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c69dc35dbcc16f5384200b8f84baa50
https://doi.org/10.1016/j.phytochem.2007.03.021
https://doi.org/10.1016/j.phytochem.2007.03.021
Autor:
Jari Vehmaanperä, Jarno Kallio, Christian Gamauf, Bernhard Seiboth, Christian P. Kubicek, Terhi Puranen, Martina Marchetti, Günter Allmaier
Publikováno v:
FEBS Journal. 274:1691-1700
The extracellular bga1-encoded β-galactosidase of Hypocrea jecorina (Trichoderma reesei) was overexpressed under the pyruvat kinase (pki1) promoter region and purified to apparent homogeneity. The monomeric enzyme is a glycoprotein with a molecular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8a72f241947e6aaa44ab38693b04a4e3
https://doi.org/10.1111/j.1742-4658.2007.05714.x
https://doi.org/10.1111/j.1742-4658.2007.05714.x
Autor:
Claudia Kamerke, Jörg Pietruszka, Lothar Elling, Natalie Hoffmann, Dong-Ju You, Manja Henze, Clement Angkawidjaja, Sabrina Ernst, Shigenori Kanaya
Publikováno v:
Journal of biotechnology. 191
The crystal structure of β-galactosidase from Bacillus circulans (BgaC) was determined at 1.8 A resolution. The overall structure of BgaC consists of three distinct domains, which are the catalytic domain with a TIM-barrel structure and two all-β d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::620130a85ce854fa12c0c523d97f6db2
https://pubmed.ncbi.nlm.nih.gov/25034434
https://pubmed.ncbi.nlm.nih.gov/25034434
Publikováno v:
International journal of biological macromolecules. 60
The crystal structure of the industrially important Aspergillus oryzae β-galactosidase has been determined at 2.60 A resolution. The Ao-β-gal is a large (985 residues) monomeric multi-domain enzyme that has a catalytic (α/β)8-barrel domain. An el
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f29a141f10c9cd1935403b41d2d7e001
https://pubmed.ncbi.nlm.nih.gov/23688418
https://pubmed.ncbi.nlm.nih.gov/23688418