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Glycoside hydrolase

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https://www.readbyqxmd.com/read/28546828/improving-the-thermostability-of-a-fungal-gh11-xylanase-via-site-directed-mutagenesis-guided-by-sequence-and-structural-analysis
#1
Nanyu Han, Huabiao Miao, Junmei Ding, Junjun Li, Yuelin Mu, Junpei Zhou, Zunxi Huang
BACKGROUND: Xylanases have been widely employed in many industrial processes, and thermophilic xylanases are in great demand for meeting the high-temperature requirements of biotechnological treatments. In this work, we aim to improve the thermostability of XynCDBFV, a glycoside hydrolase (GH) family 11 xylanase from the ruminal fungus Neocallimastix patriciarum, by site-directed mutagenesis. We report favorable mutations at the C-terminus from B-factor comparison and multiple sequence alignment...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28546425/the-first-crystal-structure-of-a-family-129-glycoside-hydrolase-from-a-probiotic-bacterium-reveals-critical-residues-and-metal-co-factors
#2
Mayo Sato, Dorothee Liebschner, Yusuke Yamada, Naohiro Matsugaki, Takatoshi Arakawa, Siobhan S Wills, Mitchell Hattie, Keith A Stubbs, Tasuku Ito, Toshiya Senda, Hisashi Ashida, Shinya Fushinobu
The α-N-acetylgalactosaminidase from the probiotic bacterium Bifidobacterium bifidum (NagBb) belongs to the glycoside hydrolase (GH) family 129 and hydrolyzes the glycosidic bond of Tn antigen (GalNAcα1-Ser/Thr). NagBb is involved in assimilation of O-glycans on mucin glycoproteins by B. bifidum in the human gastrointestinal tract, but its catalytic mechanism has remained elusive because of a lack of sequence homology around putative catalytic residues and of other structural information. Here we report the X-ray crystal structure of NagBb, representing the first GH129 family structure, solved by the single-wavelength anomalous dispersion method based on sulfur atoms of the native protein...
May 25, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28545388/chemical-and-structural-characterization-of-%C3%AE-n-acetylgalactosaminidase-i-and-ii-from-starfish-asterina-amurensis
#3
Md Harun-Or Rashid, Golam Sadik, Ahm Khurshid Alam, Toshihisa Tanaka
BACKGROUND: The marine invertebrate starfish was found to contain a novel α-N-acetylgalactosaminidase, α-GalNAcase II, which catalyzes removal of terminal α-N-acetylgalactosamine (α-GalNAc), in addition to a typical α-N-acetylgalactosaminidase, α-GalNAcase I, which catalyzes removal of terminal α-N-acetylgalactosamine (α-GalNAc) and, to a lesser extent, galactose. The interrelationship between α-GalNAcase I and α-GalNAcase II and the molecular basis of their differences in substrate specificity remain unknown...
May 25, 2017: BMC Biochemistry
https://www.readbyqxmd.com/read/28537141/evaluation-of-acceptor-selectivity-of-lactococcus-lactis-ssp-lactis-trehalose-6-phosphate-phosphorylase-in-the-reverse-phosphorolysis-and-synthesis-of-a-new-sugar-phosphate
#4
Yodai Taguchi, Wataru Saburi, Ryozo Imai, Haruhide Mori
Trehalose 6-phosphate phosphorylase (TrePP), a member of glycoside hydrolase family 65, catalyzes the reversible phosphorolysis of trehalose 6-phosphate (Tre6P) with inversion of the anomeric configuration to produce β-d-glucose 1-phosphate (β-Glc1P) and d-glucose 6-phosphate (Glc6P). TrePP in Lactococcus lactis ssp. lactis (LlTrePP) is, alongside the phosphotransferase system, involved in the metabolism of trehalose. In this study, recombinant LlTrePP was produced and characterized. It showed its highest reverse phosphorolytic activity at pH 4...
May 24, 2017: Bioscience, Biotechnology, and Biochemistry
https://www.readbyqxmd.com/read/28531185/thermal-stability-and-kinetic-constants-for-129-variants-of-a-family-1-glycoside-hydrolase-reveal-that-enzyme-activity-and-stability-can-be-separately-designed
#5
Dylan Alexander Carlin, Siena Hapig-Ward, Bill Wayne Chan, Natalie Damrau, Mary Riley, Ryan W Caster, Bowen Bethards, Justin B Siegel
Accurate modeling of enzyme activity and stability is an important goal of the protein engineering community. However, studies seeking to evaluate current progress are limited by small data sets of quantitative kinetic constants and thermal stability measurements. Here, we report quantitative measurements of soluble protein expression in E. coli, thermal stability, and Michaelis-Menten constants (kcat, KM, and kcat/KM) for 129 designed mutants of a glycoside hydrolase. Statistical analyses reveal that functional Tm is independent of kcat, KM, and kcat/KM in this system, illustrating that an individual mutation can modulate these functional parameters independently...
2017: PloS One
https://www.readbyqxmd.com/read/28528790/characterization-of-a-novel-thermostable-gh45-endoglucanase-from-chaetomium-thermophilum-and-its-biodegradation-of-pectin
#6
Qinzheng Zhou, Peng Ji, Jianye Zhang, Xue Li, Chao Han
A novel thermostable endoglucanase (CTendo45) encoding gene was cloned from Chaetomium thermophilum and heterologously expressed in Pichia pastoris. Sequence alignment indicated that the CTendo45 enzyme belonged to glycoside hydrolase family 45. The recombinant enzyme was purified by Ni(2+) affinity chromatography, and its apparent molecular mass was estimated to be 32 kDa by SDS-PAGE. The purified enzyme displayed maximum activity at 70°C and pH 4. CTendo45 was stable at 60°C for 1 h, and residual activities of 78...
May 19, 2017: Journal of Bioscience and Bioengineering
https://www.readbyqxmd.com/read/28522605/structure-function-analysis-of-human-sucrase-isomaltase-identifies-key-residues-required-for-catalytic-activity
#7
Birthe Gericke, Natalie Schecker, Mahdi Amiri, Hassan Y Naim
Sucrase-isomaltase (SI) is an intestinal membrane-associated α-glucosidase that breaks down di- and oligosaccharides to absorbable monosaccharides. SI has two homologous functional subunits (sucrase and isomaltase) that both belong to the glycoside hydrolase family 31 (GH31) and differ in substrate specificity. All GH31 enzymes share a consensus sequence harboring an aspartic acid residue as a catalytic nucleophile. Moreover, crystallographic structural analysis of isomaltase predicts that another aspartic acid residue functions as a proton donor in hydrolysis...
May 18, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28521816/biochemical-characterization-of-the-xylan-hydrolysis-profile-of-the-extracellular-endo-xylanase-from-geobacillus-thermodenitrificans-t12
#8
Martinus J A Daas, Patricia Murciano Martínez, Antonius H P van de Weijer, John van der Oost, Willem M de Vos, Mirjam A Kabel, Richard van Kranenburg
BACKGROUND: Endo-xylanases are essential in degrading hemicellulose of various lignocellulosic substrates. Hemicellulose degradation by Geobacillus spp. is facilitated by the hemicellulose utilization (HUS) locus that is present in most strains belonging to this genus. As part of the HUS locus, the xynA gene encoding an extracellular endo-xylanase is one of the few secreted enzymes and considered to be the key enzyme to initiate hemicellulose degradation. Several Geobacillus endo-xylanases have been characterized for their optimum temperature, optimum pH and generation of degradation products...
May 18, 2017: BMC Biotechnology
https://www.readbyqxmd.com/read/28515785/recombinant-expression-of-thermostable-processive-mteg5-endoglucanase-and-its-synergism-with-mtlpmo-from-myceliophthora-thermophila-during-the-hydrolysis-of-lignocellulosic-substrates
#9
Anthi Karnaouri, Madhu Nair Muraleedharan, Maria Dimarogona, Evangelos Topakas, Ulrika Rova, Mats Sandgren, Paul Christakopoulos
BACKGROUND: Filamentous fungi are among the most powerful cellulolytic organisms in terrestrial ecosystems. To perform the degradation of lignocellulosic substrates, these microorganisms employ both hydrolytic and oxidative mechanisms that involve the secretion and synergism of a wide variety of enzymes. Interactions between these enzymes occur on the level of saccharification, i.e., the release of neutral and oxidized products, but sometimes also reflected in the substrate liquefaction...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28510502/the-impact-of-steroidal-glycoalkaloids-on-the-physiology-of-phytophthora-infestans-the-causative-agent-of-potato-late-blight
#10
Paul Dahlin, Marion C Müller, Sophia Ekengren, Lauren S McKee, Vincent Bulone
Steroidal glycoalkaloids (SGAs) are plant secondary metabolites known to be toxic to animals and humans and that have putative roles in defense against pests. The proposed mechanisms of SGA toxicity are sterol-mediated disruption of membranes and inhibition of cholinesterase activity in neurons. It has been suggested that phytopathogenic microorganisms can overcome SGA toxicity by enzymatic deglycosylation of SGAs. Here, we have explored SGA-mediated toxicity toward the invasive oomycete Phytophthora infestans, the causative agent of the late blight disease in potato and tomato, as well as the potential for SGA deglycosylation by this species...
May 16, 2017: Molecular Plant-microbe Interactions: MPMI
https://www.readbyqxmd.com/read/28508385/improving-the-temperature-characteristics-and-catalytic-efficiency-of-a-mesophilic-xylanase-from-aspergillus-oryzae-aoxyn11a-by-iterative-mutagenesis-based-on-in-silico-design
#11
Xue-Qing Li, Qin Wu, Die Hu, Rui Wang, Yan Liu, Min-Chen Wu, Jian-Fang Li
To improve the temperature characteristics and catalytic efficiency of a glycoside hydrolase family (GHF) 11 xylanase from Aspergillus oryzae (AoXyn11A), its variants were predicted based on in silico design. Firstly, Gly(21) with the maximum B-factor value, which was confirmed by molecular dynamics (MD) simulation on the three-dimensional structure of AoXyn11A, was subjected to site-saturation mutagenesis. Thus, one variant with the highest thermostability, AoXyn11A(G21I), was selected from the mutagenesis library, E...
December 2017: AMB Express
https://www.readbyqxmd.com/read/28503950/the-effects-of-rapeseed-meal-and-legume-seeds-as-substitutes-for-soybean-meal-on-productivity-and-gastrointestinal-function-in-rabbits
#12
Andrzej Gugołek, Jerzy Juśkiewicz, Janusz Strychalski, Cezary Zwoliński, Ewa Żary-Sikorska, Małgorzata Konstantynowicz
The aim of this study was to determine the effects of soybean meal (SBM) substitution by a mixture of rapeseed meal (RSM), white lupine seeds (WLS) and pea seeds (PS) on productivity, nutrient digestibility, nitrogen retention and gastrointestinal function in Hyplus rabbits. The Control diet (SBM15) contained 15% SBM, whereas Diet SBM7.5 contained 7.5% SBM, 5% RSM, 4% WLS and 3% PS. In Diet SBM0, SBM was completely replaced by RSM, WLS and PS (10%, 8% and 6%, respectively). A production trial was performed on 90 Hyplus rabbits aged from 35 to 84 d (45 each sex; 953 ± 4...
May 15, 2017: Archives of Animal Nutrition
https://www.readbyqxmd.com/read/28503710/characterization-of-a-new-multifunctional-beta-glucosidase-from-musca-domestica
#13
Shu Zhang, Jian Huang, Rong Hu, Guo Guo, Xiaoli Shang, Jianwei Wu
OBJECTIVE: To engineer Pichia pastoris for heterologous production of cellulase from Musca domestica and explore its potential for industrial applications. RESULTS: A new beta-glucosidase gene (bg), encoding 562 amino acids, was cloned from M. domestica by using rapid amplification of cDNA ends. The gene bg was linked to pPICZαA and expressed in P. pastoris with a yield of 500 mg l(-1). The enzyme has the maximum activity with 27.6 U mg(-1) towards cellulose...
May 13, 2017: Biotechnology Letters
https://www.readbyqxmd.com/read/28500928/molecular-cloning-characterization-and-in-silico-analysis-of-a-thermostable-%C3%AE-glucosidase-enzyme-from-putranjiva-roxburghii-with-a-significant-activity-for-cellobiose
#14
Bibekananda Kar, Preeti Verma, Girijesh Kumar Patel, Ashwani Kumar Sharma
The native Putranjiva roxburghii family 1 glycoside hydrolase enzyme showed β-D-fucosidase activity in addition to β-D-glucosidase and β-D-galactosidase activities reported in our previous study. A single step concanvalin A affinity chromatography for native PRGH1 improved the yield and reduced the purification time. The PRGH1 gene was cloned and overexpressed in E. coli. The full length gene contained an ORF of 1617 bp encoding a polypeptide of 538 amino acids. The amino acid sequence of PRGH1 showed maximum similarities to β-glucosidases and myrosinases...
May 10, 2017: Phytochemistry
https://www.readbyqxmd.com/read/28496452/transcriptome-analyses-reveal-candidate-pod-shattering-associated-genes-involved-in-the-pod-ventral-sutures-of-common-vetch-vicia-sativa-l
#15
Rui Dong, Deke Dong, Dong Luo, Qiang Zhou, Xutian Chai, Jiyu Zhang, Wengang Xie, Wenxian Liu, Yang Dong, Yanrong Wang, Zhipeng Liu
The seed dispersion caused by pod shattering is a form of propagation used by many wild species. Loss of seeds from pod shattering is frequent in the common vetch (Vicia sativa L.), an important self-pollinating annual forage legume. However, pod shattering is one of the most important defects that limits the reproduction of the vetch in the field and the usage as a leguminous forage crop. To better understand the vetch pod shattering mechanism, we used high-throughput RNA sequencing to assess the global changes in the transcriptomes of the pod ventral sutures of shattering-susceptible and shattering-resistant vetch accessions screened from 541 vetch germplasms...
2017: Frontiers in Plant Science
https://www.readbyqxmd.com/read/28493500/conformational-analysis-of-the-mannosidase-inhibitor-kifunensine-a-quantum-mechanical-and-structural-approach
#16
Alexandra Males, Lluis Raich, Spencer J Williams, Carme Rovira, Gideon John Davies
The varied yet family-specific conformational pathways utilized by individual glycoside hydrolases (GHs) offer a tantalising prospect for the design of tight binding and specific enzyme inhibitors. A cardinal example of a GH family specific inhibitor, and one that finds widespread practical use, is the natural product kifunensine, which is a low nanomolar inhibitor selective for GH family 47 inverting a-mannosidases. Here we show, through quantum mechanical approaches, that kifunensine is restrained to a 'ring-flipped' 1C4 conformation with another accessible, but higher-energy, region around the 1,4B conformation...
May 11, 2017: Chembiochem: a European Journal of Chemical Biology
https://www.readbyqxmd.com/read/28490053/prebiotic-effect-of-xylooligosaccharides-produced-from-birchwood-xylan-by-a-novel-fungal-gh11-xylanase
#17
Manuel Nieto-Domínguez, Laura I de Eugenio, María J York-Durán, Barbara Rodríguez-Colinas, Francisco J Plou, Empar Chenoll, Ester Pardo, Francisco Codoñer, María Jesús Martínez
A fungal endoxylanase belonging to the glycoside hydrolase gene family 11 (GH11) was obtained from the ascomycete Talaromyces amestolkiae. The enzyme was purified, characterized and used to produce a mixture of xylooligosaccharides (XOS) from birchwood xylan. A notable yield of neutral XOS was obtained (28.8%) upon enzyme treatment and the mixture contained a negligible amount of xylose, having xylobiose, xylotriose and xylotetraose as its main components. The prebiotic potential of this mixture was demonstrated upon analyzing the variations in microorganisms' composition and organic acids profile in breast-fed child faeces fermentations...
October 1, 2017: Food Chemistry
https://www.readbyqxmd.com/read/28488246/potential-coordination-role-between-o-glcnacylation-and-epigenetics
#18
REVIEW
Donglu Wu, Yong Cai, Jingji Jin
Dynamic changes of the post-translational O-GlcNAc modification (O-GlcNAcylation) are controlled by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) and the glycoside hydrolase O-GlcNAcase (OGA) in cells. O-GlcNAcylation often occurs on serine (Ser) and threonine (Thr) residues of the specific substrate proteins via the addition of O-GlcNAc group by OGT. It has been known that O-GlcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms...
May 9, 2017: Protein & Cell
https://www.readbyqxmd.com/read/28479293/crystal-structure-and-biological-implications-of-a-glycoside-hydrolase-family-55-%C3%AE-1-3-glucanase-from-chaetomium-thermophilum
#19
Anastassios C Papageorgiou, Jinyin Chen, Duochuan Li
Crystal structures of a β-1,3-glucanase from the thermophilic fungus Chaetomium thermophilum were determined at 1.20 and 1.42Å resolution in the free and glucose-bound form, respectively. This is the third structure of a family 55 glycoside hydrolase (GH55) member and the second from a fungus. Based on comparative structural studies and site-directed mutagenesis, Glu654 is proposed as the catalytic acid residue. The substrate binding cleft exhibits restricted access on one side, rendering the enzyme as an exo-β-1,3-glucanase as confirmed also by thin layer chromatography experiments...
May 4, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28479043/characterization-of-a-thermostable-glycoside-hydrolase-family-36-%C3%AE-galactosidase-from-caldicellulosiruptor-bescii
#20
Areum Lee, Kyoung-Hwa Choi, Dahye Yoon, Suhkmann Kim, Jaeho Cha
The putative gene cluster involved in the degradation of the raffinose family oligosaccharides (RFO) was identified in Caldicellulosiruptor bescii. Within the cluster, the gene encoding a putative α-galactosidase (CbAga36) was cloned and expressed in Escherichia coli. Size exclusion chromatography of the purified rCbAga36 indicated that the native form was a tetramer. Its primary sequence was similar to the family of glycoside hydrolase 36. The purified recombinant CbAga36 (rCbAga36) was optimally active at pH 5...
May 4, 2017: Journal of Bioscience and Bioengineering
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