Page last updated: 2024-09-05

maltoheptaose and tryptophan

maltoheptaose has been researched along with tryptophan in 4 studies

Compound Research Comparison

Studies
(maltoheptaose)
Trials
(maltoheptaose)
Recent Studies (post-2010)
(maltoheptaose)
Studies
(tryptophan)
Trials
(tryptophan)
Recent Studies (post-2010) (tryptophan)
11403932,7629367,183

Protein Interaction Comparison

ProteinTaxonomymaltoheptaose (IC50)tryptophan (IC50)
MyeloperoxidaseHomo sapiens (human)2.25

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (25.00)18.2507
2000's3 (75.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Ford, C; Reilly, PJ; Sierks, MR; Svensson, B1
Andersen, C; Benz, R; Orlik, F1
Christensen, T; Frandsen, TP; Kaarsholm, NC; Sigurskjold, BW; Svensson, B1
Feil, SC; Gupta, A; Kemp, BE; Parker, MW; Polekhina, G; Stapleton, D; van Denderen, BJ1

Other Studies

4 other study(ies) available for maltoheptaose and tryptophan

ArticleYear
Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis.
    Protein engineering, 1993, Volume: 6, Issue:1

    Topics: Amino Acid Sequence; Aspergillus; Base Sequence; Binding Sites; Carbohydrate Sequence; Catalysis; Glucan 1,4-alpha-Glucosidase; Glucans; Isomaltose; Leucine; Maltose; Models, Chemical; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Structure-Activity Relationship; Substrate Specificity; Tryptophan

1993
Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (maltoporin) channel of Escherichia coli. II. Effect on maltose and maltooligosaccharide binding kinetics.
    Biophysical journal, 2002, Volume: 83, Issue:1

    Topics: Bacterial Outer Membrane Proteins; Biological Transport; Biophysical Phenomena; Biophysics; Carbohydrate Metabolism; Carbohydrates; Crystallography, X-Ray; Escherichia coli; Glucans; Kinetics; Lipid Bilayers; Lipids; Maltose; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oligosaccharides; Phenylalanine; Porins; Protein Binding; Receptors, Virus; Time Factors; Trisaccharides; Tryptophan; Tyrosine

2002
Physicochemical characterisation of the two active site mutants Trp(52)-->Phe and Asp(55)-->Val of glucoamylase from Aspergillus niger.
    Biochimica et biophysica acta, 2002, Dec-16, Volume: 1601, Issue:2

    Topics: Amino Acid Substitution; Aspartic Acid; Aspergillus niger; Binding Sites; Calorimetry; Glucan 1,4-alpha-Glucosidase; Glucans; Guanidine; Kinetics; Maltose; Mutation; Phenylalanine; Protein Conformation; Protein Denaturation; Sequence Deletion; Substrate Specificity; Tryptophan; Valine

2002
Structural basis for glycogen recognition by AMP-activated protein kinase.
    Structure (London, England : 1993), 2005, Volume: 13, Issue:10

    Topics: Amino Acid Sequence; AMP-Activated Protein Kinases; Animals; beta-Cyclodextrins; Binding Sites; Binding, Competitive; Carbohydrate Conformation; Catalytic Domain; Crystallography, X-Ray; Glucans; Glucose; Glycogen; Leucine; Liver; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutation; Oligosaccharides; Protein Binding; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Protein Subunits; Rats; Sequence Homology, Amino Acid; Spectrum Analysis, Raman; Tryptophan; Water

2005