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

maltohexaose and tyrosine

maltohexaose has been researched along with tyrosine in 3 studies

Compound Research Comparison

Studies
(maltohexaose)		Trials
(maltohexaose)		Recent Studies (post-2010)
(maltohexaose)		Studies
(tyrosine)		Trials
(tyrosine)		Recent Studies (post-2010) (tyrosine)
8002444,2738468,225

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (33.33)18.2507
2000's2 (66.67)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Johnson, LN; O'Reilly, M; Palm, D; Schinzel, R; Watson, KA1
Dijkhuizen, L; Dijkstra, BW; Uitdehaag, JC; van Alebeek, GJ; van Der Veen, BA1
Kamitori, S; Mizuno, M; Ohtaki, A; Sakano, Y; Tonozuka, T; Yoshida, H1

Other Studies

3 other study(ies) available for maltohexaose and tyrosine

ArticleYear
Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase.
    Nature structural biology, 1997, Volume: 4, Issue:5

    Topics: Crystallization; Crystallography, X-Ray; Escherichia coli; Glucans; Glucosyltransferases; Kinetics; Models, Molecular; Oligosaccharides; Protein Binding; Protein Conformation; Tyrosine

1997
Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity.
    Biochemistry, 2000, Jul-04, Volume: 39, Issue:26

    Topics: Bacillus; Binding Sites; Carbohydrate Sequence; Cyclodextrins; Glucans; Glucosyltransferases; Glycosylation; Models, Molecular; Molecular Mimicry; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligosaccharides; Protein Conformation; Substrate Specificity; Tyrosine

2000
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