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Showing 1 to 11 of 11 found. | Sort by date

1 Involvement of aspartic and glutamic residues in kringle-2 of tissue-type plasminogen activator in lysine binding, fibrin binding and stimulation of activity as revealed by chemical modification and oligonucleotide-directed mutagenesis
article 1990    
Author: Weening-Verhoeff, E.J.D. · Quax, P.H.A. · Leeuwen, R.T.J. van · Rehberg, E.F. · Marotti, K.R. · Verheijen, J.H.
Keywords: Health · Chemical modification · Ligand binding · Site directed mutagenesis · Amino Acid Sequence · Aspartic Acid · Base Sequence · Ethyldimethylaminopropyl Carbodiimide · Fibrin · Glutamates · Kinetics · Lysine · Molecular Sequence Data · Mutagenesis, Site-Directed · Mutation · Peptide Fragments · Plasminogen · Protein Engineering · Tissue Plasminogen Activator

2 Binding of human urokinase-type plasminogen activator to its receptor : Residues involved in species specificity and binding
article 1998    
Author: Quax, P.H.A. · Grimbergen, J.M. · Lansink, M. · Bakker, A.H.F. · Blatter, M.C. · Belin, D. · Hinsbergh, V.W.M. van · Verheijen, J.H.
Keywords: Health · Site-directed mutagenesis · Urokinase-type plasminogen activator · Urokinase-type plasminogen activator receptor · Amino Acid Sequence · Animals · Asparagine · Binding, Competitive · Cells, Cultured · Cricetinae · Endothelium, Vascular · Humans · Ligands · Mice · Molecular Sequence Data · Mutagenesis, Site-Directed · Receptors, Cell Surface · Sequence Homology, Amino Acid · Species Specificity · Swine · Tyrosine · Urinary Plasminogen Activator
[Abstract]

3 Single amino acid residue changes in subsite - 1 of inulosucrase from Lactobacillus reuteri 121 strongly influence the size of products synthesized
article 2006    
Author: Ozimek, L.K. · Kralj, S. · Kaper, T. · Maarel, M.J.E.C. van der · Dijkhuizen, L.
Keywords: Food technology · Inulosucrase · Lactobacillus reuteri · Processivity · Site-directed mutagenesis · Amino acid · Arginine · Aspartic acid · Fructan · Fructansucrase · Fructose oligosaccharide · Glutamic acid · Glycosidase · Histidine · Inulin · Inulosucrase · Levan · Lysine · Mutant protein · Oligosaccharide · Polymer · Sucrase · Sucrose · Tryptophan · Unclassified drug · Amino acid sequence · Carbohydrate synthesis · Catalysis · Concentration (parameters) · Controlled study · Enzyme active site · Enzyme activity · Enzyme specificity · Enzyme structure · Enzyme substrate · Glycosylation · Molecular recognition · Molecular size · Nonhuman · Nucleotide sequence · Protein family · Amino Acid Substitution · Binding Sites · Hexosyltransferases · Lactobacillus reuteri · Molecular Weight · Oligosaccharides · Bacillus subtilis · Bacteria (microorganisms) · Lactobacillus reuteri
[PDF] [Abstract]

4 Site-directed mutagenesis study of the three catalytic residues of the fructosyltransferases of Lactobacillus reuteri 121
article 2004    
Author: Ozimek, L.K. · Hijum, S.A.F.T. van · Koningsveld, G.A. van · Maarel, M.J.E.C. van der · Geel-Schutten, G.H. van · Dijkhuizen, L.
Keywords: Food technology · Catalytic residue · Fructosyltransferase · Inulosucrase · Levansucrase · Mutagenesis · Acid · Base · Glycosidase · Levansucrase · Mutant protein · Stabilizing agent · Sucrase · Transferase · Bacterium mutant · Enzyme activity · Nonhuman · Site directed mutagenesis · Amino Acid Motifs · Amino Acid Sequence · Amino Acid Substitution · Catalysis · Circular Dichroism · Cloning, Molecular · Conserved Sequence · Escherichia coli · Gene Expression · Genes, Bacterial · Hexosyltransferases · Kinetics · Lactobacillus · Molecular Sequence Data · Mutagenesis, Site-Directed · Sequence Homology, Amino Acid · Substrate Specificity · Bacillus subtilis · Bacteria (microorganisms) · Lactobacillus reuteri
[PDF] [Abstract]

5 Mutational analysis of the role of calcium ions in the Lactobacillus reuteri strain 121 fructosyltransferase (levansucrase and inulosucrase) enzymes
article 2005    
Author: Ozimek, L.K. · Euverink, G.J.W. · Maarel, M.J.E.C. · Dijkhuizen, L.
Keywords: Food technology · Lactobacillus reuteri · Levansucrase · Mutagenesis · Bacterial enzyme · Fructosyltransferase · Inulosucrase · Levansucrase · Metal ion · Unclassified drug · Amino acid sequence · Bacillus subtilis · Bacterial strain · Calcium binding · Calcium transport · Enzyme activity · Enzyme structure · Gram positive bacterium · Metal binding · Mutational analysis · Nonhuman · Nucleotide sequence · Priority journal · Protein family · Site directed mutagenesis · Amino Acid Sequence · Binding Sites · Calcium · Edetic Acid · Enzyme Stability · Hexosyltransferases · Ion Transport · Lactobacillus · Molecular Sequence Data · Mutation · Protein Denaturation · Sequence Alignment · Temperature
[Abstract]

6 Mutational analysis of pea lectin: Substitution of Asn125 for Asp in the monosaccharide-binding site eliminates mannose/glucose-binding activity
article 1992    
Author: Eijsden, R.R. van · Hoedemaeker, F.J. · Díaz, C.L. · Lugtenberg, B.J.J. · Sylvia Pater, B. de · Kijne, J.W.
Keywords: mutagenesis · pea lectin · sugar binding · mannose · oligodeoxyribonucleotide · pea lectin · phytohemagglutinin · amino acid sequence · binding site · chemistry · comparative study · Escherichia coli · genetics · legume · medicinal plant · metabolism · molecular genetics · nucleotide sequence · site directed mutagenesis · structure activity relation · Amino Acid Sequence · Asparagine · Aspartic Acid · Base Sequence · Binding Sites · Calcium · Comparative Study · DNA Mutational Analysis · Escherichia coli · Fabaceae · Glucose · Lectins · Manganese · Mannose · Molecular Sequence Data · Mutagenesis, Site-Directed · Oligodeoxyribonucleotides · Phytohemagglutinins · Plants, Medicinal · Sequence Alignment · Structure-Activity Relationship
[Abstract]

7 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]

8 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]

9 Exo-inulinase of Aspergillus niger N402: A hydrolytic enzyme with significant transfructosylating activity
article 2008    
Author: Goosen, C. · Maarel, M.J. E.C. van der · Dijkhuizen, L.
Keywords: Biology · Aspergillus niger · Exo-inulinase · Glycoside hydrolase · Hydrolysis · SVEVF motif · Transfructosylation · Enzymes · Escherichia coli · Hydrolysis · Polysaccharides · Purification · Sugar (sucrose) · Sugars · Water pollution · Aspergillus niger · Exo-inulinase · Glycoside hydrolase · SVEVF motif · Transfructosylation · Enzyme activity · fructan · fungal enzyme · glycosidase · hydrolase · inulinase · oligosaccharide · protein AngInuE · sucrose · article · Aspergillus niger · carbohydrate synthesis · catalysis · concentration response · enzyme activity · enzyme analysis · enzyme purification · enzyme specificity · enzyme substrate · enzyme synthesis · Escherichia coli · fungal strain · hydrolysis · molecular weight · nonhuman · nucleotide sequence · protein analysis · protein domain · site directed mutagenesis · Aspergillus niger · Escherichia coli
[Abstract]

10 Properties and applications of starch-converting enzymes of the alpha-amylase family
article 2002    
Author: Maarel, M.J.E.C. van der · Veen, B. van der · Uitdehaag, J.C.M. · Leemhuis, H. · Dijkhuizen, L.
Keywords: Nutrition · α-Amylase · Anti-staling of bread · Glycosylhydrolases · Starch industry · Starch-converting enzymes · Amino acids · Chemical bonds · Conformations · Crystallization · Enzymes · Hydrolysis · Mutagenesis · Substrates · X-ray crystallography · Amylopectin · Cyclodextrin · Cyclomaltodextrin glucanotransferase · Dextrin · Dipeptidyl carboxypeptidase · Fructose · Glucose · Glycosidase · Maltodextrin · Maltose · Maltotriose · Transferase · Bacterium · Crop · Enzyme active site · Enzyme conformation · Enzyme engineering · Enzyme mechanism · Enzyme specificity · Enzyme stability · Enzyme substrate complex · Enzyme synthesis · Food processing · Industrial production · Protein domain · Protein family · Site directed mutagenesis · Structure activity relation · Amino Acid Sequence · Biotechnology · Conserved Sequence · Glycoside Hydrolases · Glycosyltransferases · Models, Molecular · Molecular Sequence Data · Protein Conformation · Sequence Homology, Amino Acid · Substrate Specificity · Manihot esculenta · Solanum tuberosum · Triticum aestivum · Zea mays
[Abstract]

11 Testosterone 15β-hydroxylation by solvent tolerant Pseudomonas putida S12
article 2007    
Author: Ruijssenaars, H.J. · Sperling, E.M.G.M. · Wiegerinck, P.H.G. · Brands, F.T.L. · Wery, J. · Bont, J.A.M.de
Keywords: Biology · Biotechnology · CYP106A2 · Fer · Pseudomonas putida · Solvent tolerance · Steroid synthesis · Whole cell biocatalyst · Biocatalysts · Enzyme kinetics · Hydroxylation · Optimization · Solvents · Pseudomonas putida · Solvent tolerance · Steroid synthesis · Whole cell biocatalysts · Drug products · 15 beta hydroxylase · bacterial protein · cytochrome P450 · organic solvent · steroid monooxygenase · testosterone · threonine · valine · 15beta hydroxylase CYP106A2, Bacillus megaterium · 15beta-hydroxylase CYP106A2, Bacillus megaterium · solvent · article · Bacillus subtilis · biocatalyst · biotransformation · chemical structure · controlled study · high performance liquid chromatography · nonhuman · nuclear magnetic resonance · priority journal · protein expression · Pseudomonas putida · steroid hydroxylation · steroidogenesis · biological model · enzyme specificity · evaluation · gene expression regulation · genetics · hydroxylation · metabolism · site directed mutagenesis · transgenic organism · Bacillus megaterium · Bacillus subtilis · Pseudomonas putida · Bacterial Proteins · Cytochrome P-450 Enzyme System · Gene Expression Regulation, Bacterial · Hydroxylation · Models, Biological · Mutagenesis, Site-Directed · Organisms, Genetically Modified · Pseudomonas putida · Solvents · Substrate Specificity · Testosterone
[Abstract]

Search results also available in MS Excel format.

Showing 1 to 11 of 11 found. | Sort by date