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Glycoside hydrolase

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https://www.readbyqxmd.com/read/28444927/endo-%C3%AE-mannosidase-catalyzed-transglycosylation
#1
Shogo Iwamoto, Yuta Kasahara, Yayoi Yoshimura, Akira Seko, Yoichi Takeda, Yukishige Ito, Kiichiro Totani, Ichiro Matsuo
In order for facilitating the synthesis of oligosaccharides, transglycosylation reactions mediated by glycoside hydrolases have been studied in various contexts. In this study, we examined transglycosylating activity of Golgi endo-α-mannosidase. To this end, we prepared various glycosyl donors and acceptors, and recombinant human Golgi endo-α-mannosidase and its various mutants were expressed. We showed that Golgi endo-α-mannosidase was able to mediate transglycosylation from α-glycosyl-fluorides. Systematic screening of various point mutants revealed that the E407D mutant had excellent transglycosylation activity and extremely low hydrolytic activity...
April 26, 2017: Chembiochem: a European Journal of Chemical Biology
https://www.readbyqxmd.com/read/28435055/cloning-and-characterization-of-a-new-cold-adapted-and-thermo-tolerant-%C3%AE-carrageenase-from-marine-bacterium-flavobacterium-sp-ys-80-122
#2
Shangyong Li, Jianhua Hao, Mi Sun
ι-Carrageenases play a role in marine ι-carrageenan degradation, and their enzymatic hydrolysates are thought to be excellent antioxidants. In this study, we identified a new ι-carrageenase, encoded by cgiF, in psychrophilic bacterium Flavobacterium sp. YS-80-122. The deduced ι-carrageenase, CgiF, belongs to glycoside hydrolase family 82 and shows less than 40% amino acid identity with characterized ι-carrageenases. The activity of recombinant CgiF peaked at 30°C (1,207.8U/mg). Notably, CgiF is a cold-adapted ι-carrageenase, which showed 36...
April 20, 2017: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/28432475/a-shinella-%C3%AE-n-acetylglucosaminidase-of-glycoside-hydrolase-family-20-displays-novel-biochemical-and-molecular-characteristics
#3
Junpei Zhou, Zhifeng Song, Rui Zhang, Caihong Chen, Qian Wu, Junjun Li, Xianghua Tang, Bo Xu, Junmei Ding, Nanyu Han, Zunxi Huang
β-N-Acetylglucosaminidases (GlcNAcases) are important for many biological functions and industrial applications. In this study, a glycoside hydrolase family 20 GlcNAcase from Shinella sp. JB10 was expressed in Escherichia coli BL21 (DE3). Compared to many GlcNAcases, the purified recombinant enzyme (rJB10Nag) exhibited a higher specificity activity (538.8 µmol min(-1) mg(-1)) or V max (1030.0 ± 82.1 µmol min(-1) mg(-1)) toward p-nitrophenyl β-N-acetylglucosaminide and N,N'-diacetylchitobiose (specificity activity of 35...
April 21, 2017: Extremophiles: Life Under Extreme Conditions
https://www.readbyqxmd.com/read/28432102/two-distinct-%C3%AE-l-arabinofuranosidases-in-caldicellulosiruptor-species-drive-degradation-of-arabinose-based-polysaccharides
#4
Md Abu Saleh, Wen-Jie Han, Ming Lu, Bing Wang, Huayue Li, Robert M Kelly, Fu-Li Li
Species in the extremely thermophilic genus Caldicellulosiruptor can degrade unpretreated plant biomass through the action of multi-modular glycoside hydrolases. To date, most focus with these bacteria has been on hydrolysis of glucans and xylans, while biodegradation mechanism for arabinose-based polysaccharides remains unclear. Here, putative α-L-arabinofuranosidases (AbFs) were identified in Caldicellulosiruptor species by homology to less thermophilic versions of these enzymes. From this screen, an extracellular XynF was determined to be a key factor in hydrolyzing α-1,2-, α-1,3-, and α-1,5-L-arabinofuranosyl residues of arabinose-based polysaccharides...
April 21, 2017: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/28425599/the-starch-binding-domain-family-cbm41-an-in-silico-analysis-of-evolutionary-relationships
#5
Štefan Janeček, Katarína Majzlová, Birte Svensson, E Ann MacGregor
Within the CAZy database, there are 81 carbohydrate-binding module (CBM) families. A CBM represents a non-catalytic domain in a modular arrangement of glycoside hydrolases (GHs). The present in silico study has been focused on starch-binding domains from the family CBM41 that are usually part of pullulanases from the α-amylase family GH13. Currently there are more than 1,600 sequences classified in the family CBM41, almost exclusively from Bacteria, and so a study was undertaken in an effort to divide the members into relevant groups (subfamilies) and also to contribute to the evolutionary picture of family CBM41...
April 20, 2017: Proteins
https://www.readbyqxmd.com/read/28422240/zwitterionic-pyrrolidene-phosphonates-inhibitors-of-the-glycoside-hydrolase-like-phosphorylase-streptomyces-coelicolor-glgei-v279s
#6
Sri Kumar Veleti, Cecile Petit, Donald R Ronning, Steven J Sucheck
We synthesized and evaluated new zwitterionic inhibitors against glycoside hydrolase-like phosphorylase Streptomyces coelicolor (Sco) GlgEI-V279S which plays a role in α-glucan biosynthesis. Sco GlgEI-V279S serves as a model enzyme for validated anti-tuberculosis (TB) target Mycobacterium tuberculosis (Mtb) GlgE. Pyrrolidine inhibitors 5 and 6 were designed based on transition state considerations and incorporate a phosphonate on the pyrrolidine moiety to expand the interaction network between the inhibitor and the enzyme active site...
April 19, 2017: Organic & Biomolecular Chemistry
https://www.readbyqxmd.com/read/28417372/separation-and-visualization-of-glycans-by-fluorophore-assisted-carbohydrate-electrophoresis
#7
Mélissa Robb, Joanne K Hobbs, Alisdair B Boraston
Fluorophore-assisted carbohydrate electrophoresis (FACE) is a method in which a fluorophore is covalently attached to the reducing end of carbohydrates, thereby allowing visualization following high-resolution separation by electrophoresis. This method can be used for carbohydrate profiling and sequencing, as well as for the determination of the specificity of carbohydrate-active enzymes. Here, we describe and demonstrate the use of FACE to separate and visualize the glycans released following digestion of oligosaccharides by glycoside hydrolases (GHs) using two examples: (1) the digestion of chitobiose by the streptococcal β-hexosaminidase GH20C, and (2) the digestion of glycogen by the GH13 member SpuA...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28417362/analyzing-activities-of-lytic-polysaccharide-monooxygenases-by-liquid-chromatography-and-mass-spectrometry
#8
Bjørge Westereng, Magnus Ø Arntzen, Jane Wittrup Agger, Gustav Vaaje-Kolstad, Vincent G H Eijsink
Lytic polysaccharide monooxygenases perform oxidative cleavage of glycosidic bonds in various polysaccharides. The majority of LMPOs studied so far possess activity on either cellulose or chitin and analysis of these activities is therefore the main focus of this review. Notably, however, the number of LPMOs that are active on other polysaccharides is increasing. The products generated by LPMOs from cellulose are either oxidized in the downstream end (at C1) or upstream end (at C4), or at both ends. These modifications only result in small structural changes, which makes both chromatographic separation and product identification by mass spectrometry challenging...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28417358/measuring-enzyme-kinetics-of-glycoside-hydrolases-using-the-3-5-dinitrosalicylic-acid-assay
#9
Lauren S McKee
Use of the 3,5-dinitrosalicylic acid reagent allows the simple and rapid quantification of reducing sugars. The method can be used for analysis of biological samples or in the characterization of enzyme reactions. Presented here is an application of the method in measuring the kinetics of a glycoside hydrolase reaction, including the optimization of the DNSA reagent, and the production of a standard curve of absorbance and sugar concentration.
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28417357/quantitative-kinetic-characterization-of-glycoside-hydrolases-using-high-performance-anion-exchange-chromatography-hpaec
#10
Nicholas McGregor, Gregory Arnal, Harry Brumer
High-performance anion-exchange chromatography coupled to pulsed amperometric detection (HPAEC-PAD) is a powerful analytical technique enabling the high-resolution separation and sensitive quantification of oligosaccharides. Here, we describe a general method for the determination of glycoside hydrolase kinetics that harnesses the intrinsic power of HPAEC-PAD to simultaneously monitor the release of multiple products under conditions of low substrate conversion. Thus, the ability to track product release under initial-rate conditions with substrate concentrations as low as 5 μM enables the determination of Michaelis-Menten kinetics for glycosidase activities, including hydrolysis and transglycosylation...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28417356/a-low-volume-parallel-copper-bicinchoninic-acid-bca-assay-for-glycoside-hydrolases
#11
Gregory Arnal, Mohamed A Attia, Jathavan Asohan, Harry Brumer
The quantitation of liberated reducing sugars by the copper-bicinchoninic acid (BCA) assay provides a highly sensitive method for the measurement of glycoside hydrolase (GH) activity, particularly on soluble polysaccharide substrates. Here, we describe a straightforward method adapted to low-volume polymerase chain reaction (PCR) tubes which enables the rapid, parallel determination of GH kinetics in applications ranging from initial activity screening and assay optimization, to precise Michaelis-Menten analysis...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28411221/an-extracellular-cell-attached-pullulanase-confers-branched-%C3%AE-glucan-utilization-in-human-gut-lactobacillus-acidophilus
#12
Marie S Møller, Yong Jun Goh, Kasper Bøwig Rasmussen, Wojciech Cypryk, Hasan Ufuk Celebioglu, Todd R Klaenhammer, Birte Svensson, Maher Abou Hachem
Of the few predicted extracellular glycan-active enzymes, glycoside hydrolase family 13 subfamily 14 (GH13_14) pullulanases are the most common in human gut lactobacilli. These enzymes share a unique modular organization, not observed in other bacteria, featuring a catalytic module, two starch binding modules, a domain of unknown function, and a C-terminal surface layer association protein (SLAP) domain. Here we explore the specificity of a representative of this group of pullulanases, LaPul13_14 and its role in branched α-glucans metabolism in the well characterized Lactobacillus acidophilus NCFM that is widely used as a probiotic...
April 14, 2017: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/28408476/ogt-a-short-overview-of-an-enzyme-standing-out-from-usual-glycosyltransferases
#13
REVIEW
Moyira Aquino-Gil, Annick Pierce, Yobana Perez-Cervera, Edgar Zenteno, Tony Lefebvre
O-GlcNAcylation is a highly dynamic post-translational modification whose level depends on nutrient status. Only two enzymes regulate O-GlcNAcylation cycling, the glycosyltransferase OGT (O-GlcNAc transferase) and the glycoside hydrolase OGA (O-GlcNAcase), that add and remove the GlcNAc moiety to and from acceptor proteins, respectively. During the last 30 years, OGT has emerged as a master regulator of cell life with O-GlcNAcylation being found in viruses, bacteria, insects, protists and metazoans. The study of OGT in different biological systems opens new perspectives for understanding this enzyme in many kingdoms of life...
April 15, 2017: Biochemical Society Transactions
https://www.readbyqxmd.com/read/28399848/distinctive-molecular-and-biochemical-characteristics-of-a-glycoside-hydrolase-family-20-%C3%AE-n-acetylglucosaminidase-and-salt-tolerance
#14
Junpei Zhou, Zhifeng Song, Rui Zhang, Rui Liu, Qian Wu, Junjun Li, Xianghua Tang, Bo Xu, Junmei Ding, Nanyu Han, Zunxi Huang
BACKGROUND: Enzymatic degradation of chitin has attracted substantial attention because chitin is an abundant renewable natural resource, second only to lignocellulose, and because of the promising applications of N-acetylglucosamine in the bioethanol, food and pharmaceutical industries. However, the low activity and poor tolerance to salts and N-acetylglucosamine of most reported β-N-acetylglucosaminidases limit their applications. Mining for novel enzymes from new microorganisms is one way to address this problem...
April 11, 2017: BMC Biotechnology
https://www.readbyqxmd.com/read/28399167/characterization-of-the-paenibacillus-beijingensis-dsm-24997-gtfd-and-its-glucan-polymer-products-representing-a-new-glycoside-hydrolase-70-subfamily-of-4-6-%C3%AE-glucanotransferase-enzymes
#15
Joana Gangoiti, Lisa Lamothe, Sander Sebastiaan van Leeuwen, Christina Vafiadi, Lubbert Dijkhuizen
Previously we have reported that the Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 uses the 4,6-α-glucanotransferase GtfD to convert maltodextrins and starch into a reuteran-like polymer consisting of (α1→4) glucan chains connected by alternating (α1→4)/(α1→6) linkages and (α1→4,6) branching points. This enzyme constituted the single evidence for this reaction and product specificity in the GH70 family, mostly containing glucansucrases encoded by lactic acid bacteria (http://www.CAZy...
2017: PloS One
https://www.readbyqxmd.com/read/28396425/unusual-active-site-location-and-catalytic-apparatus-in-a-glycoside-hydrolase-family
#16
Jose Munoz-Munoz, Alan Cartmell, Nicolas Terrapon, Bernard Henrissat, Harry J Gilbert
The human gut microbiota use complex carbohydrates as major nutrients. The requirement for an efficient glycan degrading systems exerts a major selection pressure on this microbial community. Thus, we propose that these bacteria represent a substantial resource for discovering novel carbohydrate active enzymes. To test this hypothesis, we focused on enzymes that hydrolyze rhamnosidic bonds, as cleavage of these linkages is chemically challenging and there is a paucity of information on l-rhamnosidases. Here we screened the activity of enzymes derived from the human gut microbiota bacterium Bacteroides thetaiotaomicron, which are up-regulated in response to rhamnose-containing glycans...
April 10, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28394946/the-integrative-omics-of-white-rot-fungus-pycnoporus-coccineus-reveals-co-regulated-cazymes-for-orchestrated-lignocellulose-breakdown
#17
Shingo Miyauchi, David Navarro, Sacha Grisel, Didier Chevret, Jean-Guy Berrin, Marie-Noelle Rosso
Innovative green technologies are of importance for converting plant wastes into renewable sources for materials, chemicals and energy. However, recycling agricultural and forestry wastes is a challenge. A solution may be found in the forest. Saprotrophic white-rot fungi are able to convert dead plants into consumable carbon sources. Specialized fungal enzymes can be utilized for breaking down hard plant biopolymers. Thus, understanding the enzymatic machineries of such fungi gives us hints for the efficient decomposition of plant materials...
2017: PloS One
https://www.readbyqxmd.com/read/28393280/nmr-line-shape-analysis-of-a-multi-state-ligand-binding-mechanism-in-chitosanase
#18
Shoko Shinya, Mariana G Ghinet, Ryszard Brzezinski, Kyoko Furuita, Chojiro Kojima, Sneha Shah, Evgenii L Kovrigin, Tamo Fukamizo
Chitosan interaction with chitosanase was examined through analysis of spectral line shapes in the NMR HSQC titration experiments. We established that the substrate, chitosan hexamer, binds to the enzyme through the three-state induced-fit mechanism with fast formation of the encounter complex followed by slow isomerization of the bound-state into the final conformation. Mapping of the chemical shift perturbations in two sequential steps of the mechanism highlighted involvement of the substrate-binding subsites and the hinge region in the binding reaction...
April 9, 2017: Journal of Biomolecular NMR
https://www.readbyqxmd.com/read/28392792/a-phylogenetically-informed-comparison-of-gh1-hydrolases-between-arabidopsis-and-rice-response-to-stressors
#19
Yun-Ying Cao, Jing-Fang Yang, Tie-Yuan Liu, Zhen-Feng Su, Fu-Yuan Zhu, Mo-Xian Chen, Tao Fan, Neng-Hui Ye, Zhen Feng, Ling-Juan Wang, Ge-Fei Hao, Jianhua Zhang, Ying-Gao Liu
Glycoside hydrolases Family 1 (GH1) comprises enzymes that can hydrolyze β-O-glycosidic bond from a carbohydrate moiety. The plant GH1 hydrolases participate in a number of developmental processes and stress responses, including cell wall modification, plant hormone activation or deactivation and herbivore resistance. A large number of members has been observed in this family, suggesting their potential redundant functions in various biological processes. In this study, we have used 304 sequences of plant GH1 hydrolases to study the evolution of this gene family in plant lineage...
2017: Frontiers in Plant Science
https://www.readbyqxmd.com/read/28392148/molecular-insight-into-evolution-of-symbiosis-between-breast-fed-infants-and-a-member-of-the-human-gut-microbiome-bifidobacterium-longum
#20
Chihaya Yamada, Aina Gotoh, Mikiyasu Sakanaka, Mitchell Hattie, Keith A Stubbs, Ayako Katayama-Ikegami, Junko Hirose, Shin Kurihara, Takatoshi Arakawa, Motomitsu Kitaoka, Shujiro Okuda, Takane Katayama, Shinya Fushinobu
Breast-fed infants generally have a bifidobacteria-rich microbiota with recent studies indicating that human milk oligosaccharides (HMOs) selectively promote bifidobacterial growth. Bifidobacterium bifidum possesses a glycoside hydrolase family 20 lacto-N-biosidase for liberating lacto-N-biose I from lacto-N-tetraose, an abundant HMO unique to human milk, while Bifidobacterium longum subsp. longum has a non-classified enzyme (LnbX). Here, we determined the crystal structure of the catalytic domain of LnbX and provide evidence for creation of a novel glycoside hydrolase family, GH136...
April 20, 2017: Cell Chemical Biology
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