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1 Three-way stabilization of the covalent intermediate in amylomaltase, an alpha-like transglycosylase
article 2007    
Author: Barends, T.R.M. · Bultema, J.B. · Kaper, T. · Maarel, M.J.E.C. van der · Dijkhuizen, L. · Dijkstra, B.W.
Keywords: Biology · Amylomaltase · Glucans · Glycosyl hydrolases · Conformations · Crystallography · Hydrolysis · Nucleophiles · Oligosaccharides · Polysaccharides · Synthesis (chemical) · Enzyme activity · Food technology · X ray crystallography · alpha-Amylase · Crystallography, X-Ray · Enzyme Stability · Glycogen Debranching Enzyme System · Glycoside Hydrolases · Models, Molecular
[Abstract]

2 Changes at the KinA PAS-A dimerization interface influence histidine kinase function
article 2008    
Author: Lee, J. · Tomchick, D.R. · Brautigam, C.A. · Machius, M. · Kort, R. · Hellingwerf, K.J. · Gardner, K.H.
Keywords: Biology · Bacteria · Catalyst activity · Crystal structure · Dimerization · Bacillus subtilis KinA protein · Histidine kinase function · Proteins · X ray · Amino Acid Sequence · Bacillus subtilis · Bacterial Proteins · Crystallography, X-Ray · Dimerization · Models, Molecular · Molecular Sequence Data · Protein Conformation · Protein Kinases · Bacillus subtilis · Bacteria (microorganisms)
[Abstract]

3 Examining the role of glutamic acid 183 in chloroperoxidase catalysis
article 2003    
Author: Yi, X. · Conesa, A. · Punt, P.J. · Hager, L.P.
Keywords: Biology · Biotechnology · Catalysis · Genetic engineering · Organic acids · X ray crystallography · Active sites · Enzymes · Chloride peroxidase · Clutamic acid · Histidine · Hydrogen peroxide · Natural product · Epoxidase · Oxidoreductase · Amino acid substitution · Animal cell · Asymmetric catalysis · Chlorination · Enzyme active site · Enzyme activity · Epoxidation · Genetic analysis · Hydrophobicity · Nonhuman · Plasmid · Site directed mutagenesis · X ray crystallography · Chemistry · Circular dichroism · Enzymology · Immunoblotting · Ion exchange chromatography · Isoelectric focusing · Metabolism · PH · polyacrylamide gel electrophoresis · Animalia · Aspergillus · Aspergillus niger · Catalase · Catalysis · Chloride Peroxidase · Chlorine · Chromatography, Ion Exchange · Circular Dichroism · Crystallography, X-Ray · Electrophoresis, Polyacrylamide Gel · Fungi · Glutamic Acid · Histidine · Hydrogen-Ion Concentration · Immunoblotting · Isoelectric Focusing · Mutation · Oxidoreductases · Plasmids
[PDF] [Abstract]

4 Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site
article 2003    
Author: Arand, M. · Hallberg, B.M. · Zou, J. · Bergfors, T. · Oesch, F. · Werf, M.J. van der · Bont, J.A.M. de · Jones, T.A. · Mowbray, S.L.
Keywords: Biology · Biotechnology · Crystal structure · Enantioselectivity · Epoxide hydrolase · Mechanism · Monoterpene degradation · bacterial enzyme · limonene 1,2 epoxide hydrolase · selenomethionine · unclassified drug · valpromide · alpha helix · article · beta sheet · catalysis · chemical reaction · crystal structure · detoxification · drug protein binding · enantioselectivity · enzyme active site · enzyme metabolism · enzyme structure · enzyme substrate complex · nonhuman · priority journal · reaction analysis · Rhodococcus erythropolis · site directed mutagenesis · Amino Acid Sequence · Bacterial Proteins · Catalytic Domain · Crystallography, X-Ray · Dimerization · Epoxide Hydrolases · Models, Molecular · Molecular Sequence Data · Mutagenesis, Site-Directed · Protein Subunits · Recombinant Proteins · Rhodococcus · Sequence Homology, Amino Acid · Actinobacteria (class) · Bacteria (microorganisms) · Rhodococcus · Rhodococcus erythropolis · uncultured actinomycete
[Abstract]

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