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1. Full Text Exploiting the aglycon promiscuity of glycosyltransferase Bs-YjiC from Bacillus subtilis and its application in synthesis of glycosides
by Dai, Longhai and Li, Jiao and Yao, Peiyuan and Zhu, Yueming and Men, Yan and Zeng, Yan and Yang, Jiangang and Sun, Yuanxia
Journal of biotechnology, ISSN 0168-1656, 04/2017, Volume 248, pp. 69 - 76
Glycosylation | Aglycon promiscuity | Glycosyltransferase sucrose synthase | Natural products | Bacillus subtilis 168 | Sucrose synthase | Glycosyltransferase | Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Science & Technology | Recombinant Proteins - metabolism | Glycosyltransferases - chemistry | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Stilbenes - metabolism | Bacillus subtilis - enzymology | Recombinant Proteins - genetics | Stilbenes - chemistry | Bacillus subtilis - genetics | Glycosyltransferases - metabolism | Escherichia coli - genetics | Glycosides - metabolism | Bacterial Proteins - metabolism | Glycosyltransferases - genetics | Glycosides - chemistry | Promiscuity | Arabidopsis thaliana | Transferases | Escherichia coli | Cellulose | Physiological aspects | Glucose | Mass spectrometry | High performance liquid chromatography | Dextrose | Index Medicus
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2. Full Text SEDS proteins are a widespread family of bacterial cell wall polymerases
by Meeske, Alexander J and Riley, Eammon P and Robins, William P and Uehara, Tsuyoshi and Mekalanos, John J and Kahne, Daniel and Walker, Suzanne and Kruse, Andrew C and Bernhardt, Thomas G and Rudner, David Z
Nature (London), ISSN 0028-0836, 08/2016, Volume 537, Issue 7622, pp. 634 - 638
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Peptidoglycan Glycosyltransferase - metabolism | Bacillus subtilis - cytology | Peptidoglycan Glycosyltransferase - chemistry | Penicillin-Binding Proteins - classification | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Polymerization | Penicillin-Binding Proteins - genetics | Bacillus subtilis - enzymology | Cell Wall - chemistry | Penicillin-Binding Proteins - metabolism | Oligosaccharides - pharmacology | Peptidoglycan - biosynthesis | Peptidoglycan Glycosyltransferase - genetics | Phenotype | Bacillus subtilis - growth & development | Cell Division | Cell Wall - metabolism | Drug Design | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Drug Resistance, Bacterial - drug effects | Mutation | Bacillus subtilis - drug effects | Physiological aspects | Bacillus subtilis | Bacterial cell walls | Proteins | Antigens | Enzymes | Bacterial infections | Peptides | Penicillin | Bacteria | Lipids | Biosynthesis | Index Medicus
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3. Full Text The penicillin‐binding proteins: structure and role in peptidoglycan biosynthesis
by Sauvage, Eric and Kerff, Frédéric and Terrak, Mohammed and Ayala, Juan A and Charlier, Paulette
FEMS microbiology reviews, ISSN 0168-6445, 03/2008, Volume 32, Issue 2, pp. 234 - 258
3D structure | transpeptidase | penicillin‐binding | transglycosylase | peptidoglycan synthesis | Peptidoglycan synthesis | Transglycosylase | Penicillin-binding | Transpeptidase | Life Sciences & Biomedicine | Microbiology | Science & Technology | Protein Structure, Tertiary | Bacteria - metabolism | Peptidyl Transferases - metabolism | Bacteria - chemistry | Multienzyme Complexes - classification | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Glycosyltransferases - chemistry | Penicillin-Binding Proteins - classification | Peptidyl Transferases - chemistry | Bacterial Proteins - chemistry | Multienzyme Complexes - metabolism | Penicillin-Binding Proteins - metabolism | Peptide Hydrolases - chemistry | Multienzyme Complexes - chemistry | Peptidoglycan - biosynthesis | Glycosyltransferases - metabolism | beta-Lactams - pharmacology | Penicillin-Binding Proteins - chemistry | Bacterial Proteins - metabolism | Bacterial Proteins - classification | beta-Lactamases - metabolism | Peptide Hydrolases - metabolism | Physiological aspects | Peptidoglycans | Index Medicus
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4. Full Text Structure, mechanism and engineering of plant natural product glycosyltransferases
by Wang, Xiaoqiang
FEBS letters, ISSN 0014-5793, 10/2009, Volume 583, Issue 20, pp. 3303 - 3309
Plant natural product | Deglycosylation | Glycosylation | Glycosyltransferase | Enzyme engineering | UDP | UGT | glycosyltransferase | uridine diphosphate | uridine diphosphate glycosyltransferase | GT | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Protein Structure, Tertiary | Amino Acid Sequence | Biological Products - genetics | Glycosyltransferases - chemistry | Humans | Molecular Sequence Data | Crystallography, X-Ray | Sequence Homology, Amino Acid | Biological Products - chemistry | Glycosyltransferases - metabolism | Plants - metabolism | Sequence Alignment | Animals | Protein Engineering | Molecular Structure | Glycosyltransferases - genetics | Plants - chemistry | Index Medicus
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5. Full Text An Evolving Hierarchical Family Classification for Glycosyltransferases
by Coutinho, Pedro M and Deleury, Emeline and Davies, Gideon J and Henrissat, Bernard
Journal of molecular biology, ISSN 0022-2836, 2003, Volume 328, Issue 2, pp. 307 - 317
glycosyltransferases | protein families | modular structure | classification | genomic annotations | Genomic annotations | Protein families | Classification | Glycosyltransferases | Modular structure | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Genomics | Glycosyltransferases - chemistry | Humans | Models, Molecular | Substrate Specificity | Terminology as Topic | Protein Folding | Amino Acid Motifs | Sequence Homology, Amino Acid | Glycosyltransferases - metabolism | Animals | Glycosyltransferases - classification | Conserved Sequence | Glycosyltransferases - genetics | Enzymes | Hydrolases | Cell research | Polysaccharides | Transferases | Index Medicus
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6. Full Text Cwp19 is a novel lytic transglycosylase involved in stationary-phase autolysis resulting in toxin release in clostridium difficile
by Wydau-Dematteis, Sandra and El Meouche, Imane and Courtin, Pascal and Hamiot, Audrey and Lai-Kuen, René and Saubaméa, Bruno and Fenaille, François and Butel, Marie-José and Pons, Jean-Louis and Dupuy, Bruno and Chapot-Chartier, Marie-Pierre and Peltier, Johann
mBio, ISSN 2161-2129, 05/2018, Volume 9, Issue 3, pp. 1 - 19
Peptidoglycan | Surface proteins | Toxins | Lytic transglycosylase | Autolysins | Clostridium difficile | Life Sciences & Biomedicine | Microbiology | Science & Technology | Catalytic Domain | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Humans | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Clostridium difficile - genetics | Cell Wall - genetics | Peptidoglycan Glycosyltransferase - genetics | Clostridium Infections - microbiology | Bacteriolysis | Clostridium difficile - physiology | Cell Wall - metabolism | Clostridium difficile - enzymology | Bacterial Proteins - metabolism | Clostridium difficile - growth & development | Gene Expression Regulation, Bacterial | Index Medicus | Cell Wall | Life Sciences | Microbiology and Parasitology | Clostridium Infections | Peptidoglycan Glycosyltransferase | Bacterial Proteins | peptidoglycan | lytic transglycosylase | autolysins | surface proteins | toxins
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