Compounds > maltohexaose
Page last updated: 2024-09-04

maltohexaose and tryptophan

maltohexaose has been researched along with tryptophan in 4 studies

Compound Research Comparison

Studies
(maltohexaose)		Trials
(maltohexaose)		Recent Studies (post-2010)
(maltohexaose)		Studies
(tryptophan)		Trials
(tryptophan)		Recent Studies (post-2010) (tryptophan)
8002432,7629367,183

Protein Interaction Comparison

ProteinTaxonomymaltohexaose (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
Blennow, A; Morell, MK; Viksø-Nielsen, A1
Feil, SC; Gupta, A; Kemp, BE; Parker, MW; Polekhina, G; Stapleton, D; van Denderen, BJ1
Akiba, T; Haga, K; Harata, K; Kanai, R; Yamane, K1
Kamitori, S; Mizuno, M; Ohtaki, A; Sakano, Y; Tonozuka, T; Yoshida, H1

Other Studies

4 other study(ies) available for maltohexaose and tryptophan

ArticleYear
Alpha-glucan binding of potato-tuber starch-branching enzyme I as determined by tryptophan fluorescence quenching, affinity electrophoresis and steady-state kinetics.
    European journal of biochemistry, 1998, Mar-01, Volume: 252, Issue:2

    Topics: 1,4-alpha-Glucan Branching Enzyme; Amylopectin; Amylose; Binding Sites; Binding, Competitive; Cyclodextrins; Glucans; Kinetics; Oligosaccharides; Plant Proteins; Protein Binding; Solanum tuberosum; Spectrometry, Fluorescence; Tryptophan

1998
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
Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.
    Protein science : a publication of the Protein Society, 2006, Volume: 15, Issue:3

    Topics: alpha-Glucosidases; Bacillus; Bacterial Proteins; Binding Sites; Catalytic Domain; Hordeum; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Oligosaccharides; Tryptophan

2006
Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft.
    Carbohydrate research, 2006, Jun-12, Volume: 341, Issue:8

    Topics: Alanine; alpha-Amylases; Amino Acid Substitution; Amino Acids, Aromatic; Binding Sites; Catalysis; Crystallography, X-Ray; Dimerization; Hydrogen Bonding; Hydrolysis; Kinetics; Micromonosporaceae; Models, Molecular; Oligosaccharides; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Substrate Specificity; Tryptophan; Tyrosine; Water

2006