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1. Full Text A novel β‐xylosidase structure from Geobacillus thermoglucosidasius: the first crystal structure of a glycoside hydrolase family GH52 enzyme reveals unpredicted similarity to other glycoside hydrolase folds
by Espina, Giannina and Eley, Kirstin and Pompidor, Guillaume and Schneider, Thomas R and Crennell, Susan J and Danson, Michael J
Acta Crystallographica Section D, ISSN 1399-0047, 05/2014, Volume 70, Issue 5, pp. 1366 - 1374
Geobacillus thermoglucosidasius is a thermophilic bacterium that is able to ferment both C6 and C5 sugars to produce ethanol. During growth on hemicellulose... 
β‐xylosidase | GH family 52 | Geobacillus thermoglucosidasius | fold conservation | retaining mechanism | thermophile | β-xylosidase | CRYSTALLOGRAPHY | BIOPHYSICS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | Catalytic Domain | Disaccharides - metabolism | Escherichia coli - genetics | Xylosidases - metabolism | Cloning, Molecular | Xylosidases - chemistry | Xylosidases - genetics | Models, Molecular | Crystallography, X-Ray | Protein Conformation | Geobacillus - enzymology | Disaccharides - chemistry | Enzymes | Addition polymerization | Similarity | Glycosides | Ethyl alcohol | Biomass | Crystal structure | Recombinant
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2. Full Text Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)
by Aspeborg, Henrik and Coutinho, Pedro M and Wang, Yang and Brumer, Harry and Henrissat, Bernard and Skolan för bioteknologi (BIO) and KTH and Glykovetenskap
BMC Evolutionary Biology, ISSN 1471-2148, 2012, Volume 12, Issue 1, p. 186
Background: The large Glycoside Hydrolase family 5 (GH5) groups together a wide range of enzymes acting on beta-linked oligo- and polysaccharides, and... 
Phylogenetic analysis | Protein evolution | Subfamily classification | Functional prediction | Glycoside hydrolase family 5 | Glycogenomics | Enzyme evolution | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | BETA-MANNANASE | THERMOASCUS-AURANTIACUS | CELLULASE | EVOLUTIONARY BIOLOGY | ENDOGLUCANASE | SEQUENCE | GENETICS & HEREDITY | BOUND FORMS | THERMOTOGA-MARITIMA | INSIGHTS | Animals | Cell Wall - metabolism | Glycoside Hydrolases - genetics | Glycoside Hydrolases - chemistry | Substrate Specificity | Glycoside Hydrolases - classification | Cell Wall - chemistry | Glycoside Hydrolases - metabolism | Phylogeny | Eukaryota - enzymology | Evolution, Molecular | Polysaccharides - metabolism | Physiological aspects | Enzymes | Molecular evolution | Hydrolases | Research | Natural history | Polysaccharides | Signal transduction | Carbohydrates | Number systems | Cellulase | Colleges & universities | Classification | Phylogenetics | Genomes | Life Sciences | Quantitative Methods | Biochemistry, Molecular Biology | Biological Sciences | Bioinformatik och systembiologi | Bioinformatics and Systems Biology | Naturvetenskap | Biologiska vetenskaper | Natural Sciences
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3. Full Text Endo-fucoidan hydrolases from glycoside hydrolase family 107 (GH107) display structural and mechanistic similarities to α-l-fucosidases from GH29
by Vickers, Chelsea and Vickers, Chelsea and Liu, Feng and Liu, Feng and Abe, Kento and Abe, Kento and Salama-Alber, Orly and Salama-Alber, Orly and Jenkins, Meredith and Jenkins, Meredith and Springate, Christopher M.K and Springate, Christopher M K and Burke, John E and Burke, John E and Withers, Stephen G and Boraston, Alisdair B and Boraston, Alisdair B
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 47, pp. 18296 - 18308
Fucoidans are chemically complex and highly heterogeneous sulfated marine fucans from brown macro algae. Possessing a variety of physicochemical and biological... 
enzyme | X-ray crystallography | enzyme catalysis | glycoside hydrolase | polysaccharide | enzyme mechanism | alpha-L-Fucosidase - genetics | Catalytic Domain | Gammaproteobacteria - enzymology | Multigene Family | alpha-L-Fucosidase - metabolism | Glycoside Hydrolases - genetics | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Polysaccharides - metabolism | Gammaproteobacteria - chemistry | alpha-L-Fucosidase - chemistry | Glycoside Hydrolases - chemistry | Bacterial Proteins - metabolism | Gammaproteobacteria - genetics | Catalysis | Glycoside Hydrolases - metabolism
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4. Full Text Glycoside hydrolase DisH from Desulfovibrio vulgaris degrades the N‐acetylgalactosamine component of diverse biofilms
by Zhu, Lei and Poosarla, Venkata G and Song, Sooyeon and Wood, Thammajun L and Miller, Daniel S and Yin, Bei and Wood, Thomas K
Environmental Microbiology, ISSN 1462-2912, 06/2018, Volume 20, Issue 6, pp. 2026 - 2037
Summary Biofilms of sulfate‐reducing bacteria (SRB) produce H2S, which contributes to corrosion. Although bacterial cells in biofilms are cemented together,... 
ACTINOBACILLUS-ACTINOMYCETEMCOMITANS | EXOPOLYSACCHARIDE | MATRIX | POLYSACCHARIDE SYNTHESIS | BACILLUS-SUBTILIS | PSEUDOMONAS-AERUGINOSA | EXTRACELLULAR DNA | ESCHERICHIA-COLI | MICROBIOLOGY | IDENTIFICATION | SULFATE-REDUCING BACTERIA | Enzymes | Polysaccharides | Analysis | Escherichia coli | Genomics | Physiological aspects | Bacteria | Hydrolases | Sulfates | Corrosion and anti-corrosives | Glucosamine | Addition polymerization | Genomes | pH effects | Bacterial corrosion | Proteins | Hydrogen sulfide | E coli | Exopolysaccharides | Desulfovibrio | Dispersal | Glycosides | Pseudomonas aeruginosa | Polymers | Hydrolase | Extracellular | Dispersion | Cells | Substrates | Biofilms | Corrosion | Sulfate | Glycoside hydrolase
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5. Full Text Crystal structure of glycoside hydrolase family 127 β-l-arabinofuranosidase from Bifidobacterium longum
by Ito, Yukishige and Ito, Tasuku and Saikawa, Kyo and Kim, Seonah and Fujita, Kiyotaka and Ishiwata, Akihiro and Kaeothip, Sophon and Arakawa, Takatoshi and Wakagi, Takayoshi and Beckham, Gregg T and Fushinobu, Shinya
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 04/2014, Volume 447, Issue 1, pp. 32 - 37
Enzymes acting on β-linked arabinofuranosides have been unknown until recently, in spite of wide distribution of β- -arabinofuranosyl oligosaccharides in plant... 
Quantum mechanical calculations | Retaining glycoside hydrolase | Plant polysaccharide | Human gut bacteria | DUF1680 | Crystal structure | EXTENSIN | BIOPHYSICS | BIOCHEMISTRY & MOLECULAR BIOLOGY | INHIBITORS | MODEL | ENERGIES | Protein Structure, Tertiary | Amino Acid Sequence | Catalytic Domain | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Cysteine - chemistry | Zinc - chemistry | Arabinose - analogs & derivatives | Quantum Theory | Sequence Alignment | Arabinose - metabolism | Glycoside Hydrolases - chemistry | Bifidobacterium - enzymology | Glycoside Hydrolases - metabolism | Glutamic Acid - chemistry
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6. Full Text The First Structure of a Glycoside Hydrolase Family 61 Member, Cel61B from Hypocrea jecorina, at 1.6 Å Resolution
by Karkehabadi, Saeid and Hansson, Henrik and Kim, Steve and Piens, Kathleen and Mitchinson, Colin and Sandgren, Mats
Journal of Molecular Biology, ISSN 0022-2836, 2008, Volume 383, Issue 1, pp. 144 - 154
The glycoside hydrolase (GH) family 61 is a long-recognized, but still recondite, class of proteins, with little known about the activity, mechanism or... 
Cel61B | Hypocrea jecorina | Trichoderma reesei | glycoside hydrolase family 61 | protein crystal structure | Hypocrea - enzymology | Glycoside Hydrolases - genetics | Molecular Sequence Data | Crystallography, X-Ray | DNA Primers - genetics | Trichoderma - enzymology | Base Sequence | Hypocrea - genetics | Glycoside Hydrolases - chemistry | Genes, Fungal | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Nickel - chemistry | Protein Structure, Secondary | Models, Molecular | Recombinant Proteins - chemistry | Glycoside Hydrolases - classification | Recombinant Proteins - genetics | Trichoderma - genetics | Static Electricity | Protein Folding | Sequence Homology, Amino Acid | Protein Processing, Post-Translational | Glycoside Hydrolases - metabolism | Physiological aspects | Enzymes | Hydrolases | Structure | Crystals
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7. Full Text Novel β-1, 4-mannanase belonging to a new glycoside hydrolase family in Aspergillus nidulans
by Shimizu, Motoyuki and Kaneko, Yuhei and Ishihara, Saaya and Mochizuki, Mai and Sakai, Kiyota and Yamada, Miyuki and Murata, Shunsuke and Itoh, Eriko and Yamamoto, Tatsuya and Sugimura, Yu and Hirano, Tatsuya and Takaya, Naoki and Kobayashi, Tetsuo and Kato, Masashi
Journal of Biological Chemistry, ISSN 0021-9258, 11/2015, Volume 290, Issue 46, pp. 27914 - 27927
Many filamentous fungi produce beta-mannan-degrading beta-1,4-mannanases that belong to the glycoside hydrolase 5 (GH5) and GH26 families. Here we identified a... 
TRANSCRIPTIONAL REGULATOR | BIOCHEMICAL ANALYSES | TRANSGLYCOSYLATION CAPACITY | MECHANISM | MANNAN UTILIZATION SYSTEM | ENZYMES | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLANT-CELL WALL | BETA-MANNANASES | BINDING | CELLULASE | Fungal Proteins - chemistry | Amino Acid Sequence | Mannosidases - chemistry | Aspergillus nidulans - genetics | Molecular Sequence Data | Mannosidases - classification | Fungal Proteins - genetics | Phylogeny | Fungal Proteins - classification | beta-Mannosidase - classification | Sequence Analysis, Protein | Mannans - chemistry | Oligosaccharides - chemistry | Mannosidases - genetics | Aspergillus nidulans - enzymology | Catalysis | beta-Mannosidase - genetics | beta-Mannosidase - chemistry | Aspergillus | oligosaccharide | transcription regulation | glycoside hydrolase | Microbiology | polysaccharide | fungi | biodegradation
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8. Full Text An inverting β-1,2-mannosidase belonging to glycoside hydrolase family 130 from Dyadobacter fermentans
by Nihira, Takanori and Chiku, Kazuhiro and Suzuki, Erika and Nishimoto, Mamoru and Fushinobu, Shinya and Kitaoka, Motomitsu and Ohtsubo, Ken’ichi and Nakai, Hiroyuki
FEBS Letters, ISSN 0014-5793, 11/2015, Volume 589, Issue 23, pp. 3604 - 3610
The glycoside hydrolase family (GH) 130 is composed of inverting phosphorylases that catalyze reversible phosphorolysis of β- -mannosides. Here we report a... 
β-1,2-Mannooligosaccharide | β-1,2-Mannosidase | Glycoside hydrolase family 130 | glycoside hydrolase family | α-d-mannose 1-phosphate | polyacrylamide-gel electrophoresis | αMan1P | PAGE | inorganic phosphate | CELLOBIOSE 2-EPIMERASE | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | beta-1,2-Mannosidase | ENZYMATIC-SYNTHESIS | MECHANISMS | MANNAN CATABOLIC PATHWAY | DISCOVERY | CELL BIOLOGY | BIOPHYSICS | beta-1,2-Mannooligosaccharide | PURIFICATION | MANNOSE | BACTERIUM | 4-O-BETA-D-MANNOSYL-D-GLUCOSE PHOSPHORYLASE | Cytophagaceae - enzymology | Mannosidases - chemistry | Catalytic Domain | Biocatalysis | Stereoisomerism | Models, Molecular | Substrate Specificity | Mannosidases - metabolism | Phylogeny | Hydrolysis | Mannose - metabolism | Mannosidases - genetics | Mannosidases - isolation & purification | Kinetics | Mutation | Mannose - chemistry
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9. Full Text Thermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of action, and products formed
by Palomo, Marta and Pijning, Tjaard and Booiman, Thijs and Dobruchowska, Justyna M and van der Vlist, Jeroen and Kralj, Slavko and Planas, Antoni and Loos, Katja and Kamerling, Johannis P and Dijkstra, Bauke W and van der Maarel, Marc J. E. C and Dijkhuizen, Lubbert and Leemhuis, Hans
Journal of biological chemistry, ISSN 0021-9258, 2011, Volume 286, Issue 5, pp. 3520 - 3530
Branching enzyme (EC 2.4.1.18; glycogen branching enzyme; GBE) catalyzes the formation of α1,6-branching points in glycogen. Until recently it was believed... 
4-ALPHA-GLUCANOTRANSFERASE | THERMOCOCCUS-LITORALIS | EVOLUTION | MARKER | BACTERIAL GLYCOGEN | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | PROTEINS | PHOSPHORYLASE | Hydrolysis | Thermus thermophilus - enzymology | 1,4-alpha-Glucan Branching Enzyme - metabolism | Catalytic Domain | 1,4-alpha-Glucan Branching Enzyme - chemistry | Cloning, Molecular - methods | Glycoside Hydrolases - chemistry | Substrate Specificity | Crystallography, X-Ray | Protein Conformation | Glycoside Hydrolases - metabolism | Enzyme Mechanisms | Thermus thermophilus | Family GH57 | Glycogen | X-ray Crystallography | Starch | Carbohydrate Processing | Protein Structure | Enzymology | Glycoside Hydrolase | Branching Enzyme
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10. Full Text Peptidoglycan Hydrolases of Escherichia coli
by Jean van Heijenoort
Microbiology and Molecular Biology Reviews, ISSN 1092-2172, 12/2011, Volume 75, Issue 4, pp. 636 - 663
Article Usage Stats Services MMBR Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
L-ALANINE AMIDASE | GLUTAMYL-MESO-DIAMINOPIMELATE | PENICILLIN-BINDING-PROTEINS | SOLUBLE LYTIC TRANSGLYCOSYLASE | ALANYL-D-ALANINE | POLYACRYLAMIDE-GEL ELECTROPHORESIS | BETA-LACTAM ANTIBIOTICS | MICROBIOLOGY | WIRKUNGSMECHANISMUS VON PENICILLIN | CELL-WALL PEPTIDOGLYCAN | TEMPERATURE-SENSITIVE MUTANTS | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Escherichia coli - enzymology | Escherichia coli - genetics | Peptide Hydrolases - genetics | Cell Wall - metabolism | Glycoside Hydrolases - genetics | Cell Wall - chemistry | Glycoside Hydrolases - metabolism | Mutation | N-Acetylmuramoyl-L-alanine Amidase - genetics | Bacteriolysis - physiology | Peptide Hydrolases - metabolism | Microbial enzymes | Escherichia coli | Peptidoglycans | Physiological aspects | Microbiological synthesis | Enzyme binding | Research | Chemical properties | Structure | Reviews
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11. Full Text Molecular basis of arabinobio-hydrolase activity in phytopathogenic fungi. Crystal structure and catalytic mechanism of Fusarium graminearum GH93 EXO-α-L-arabinanase
by Carapito, Raphaël and Imberty, Anne and Jeltsch, Jean-Marc and Byrns, Simon C and Tam, Pui-Hang and Lowary, Todd L and Varrot, Annabelle and Phalip, Vincent
Journal of Biological Chemistry, ISSN 0021-9258, 05/2009, Volume 284, Issue 18, pp. 12285 - 12296
The phytopathogenic fungus Fusarium graminearum secretes a very diverse pool of glycoside hydrolases (GHs) aimed at degrading plant cell walls.... 
ALPHA-L-ARABINOFURANOSIDASE | BETA-PROPELLER | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ARABINANASE 43A | ENZYMATIC GLYCOSIDE HYDROLYSIS | PLANT-CELL-WALL | BACTERIAL SIALIDASES | PENICILLIUM-CHRYSOGENUM EXO-1,5-ALPHA-L-ARABINANASE | FUSARIUM-GRAMINEARUM | ARABINOXYLAN-ARABINOFURANOHYDROLASE | Fungal Proteins - chemistry | Polysaccharides | Models, Chemical | Glycoside Hydrolases - chemistry | Models, Molecular | Nuclear Magnetic Resonance, Biomolecular | Protein Structure, Secondary - physiology | Crystallography, X-Ray | Fusarium - enzymology | Protein Structure, Tertiary - physiology | Index Medicus
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