Compounds > acebutolol

acebutolol and maltal

acebutolol has been researched along with maltal in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19901 (20.00)18.7374
1990's4 (80.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Brewer, CF; Chiba, S; Hehre, EJ; Kitahata, S1
Brewer, CF; Hehre, EJ; Kitahata, S1
Degano, M; Hehre, EJ; Mikami, B; Sacchettini, JC1
Kunikata, T; Nishimura, S; Nitta, Y1
Palau, J; Pujadas, G1

Other Studies

5 other study(ies) available for acebutolol and maltal

ArticleYear
Mechanism of maltal hydration catalyzed by beta-amylase: role of protein structure in controlling the steric outcome of reactions catalyzed by a glycosylase.
    Biochemistry, 1991, Jul-09, Volume: 30, Issue:27

    Topics: beta-Amylase; Catalysis; Chromatography, Gas; Deuterium; Glycine max; Isotopes; Kinetics; Magnetic Resonance Spectroscopy; Maltose; Protein Conformation; Solanum tuberosum; Water

1991
Catalytic flexibility of glycosylases. The hydration of maltal by beta-amylase to form 2-deoxymaltose.
    The Journal of biological chemistry, 1986, Feb-15, Volume: 261, Issue:5

    Topics: Amylases; beta-Amylase; Carbohydrate Conformation; Deuterium; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Maltose; Plant Proteins; Substrate Specificity

1986
Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis.
    Biochemistry, 1994, Jun-28, Volume: 33, Issue:25

    Topics: Amino Acid Sequence; beta-Amylase; Binding Sites; Crystallography, X-Ray; Glycine max; Ligands; Maltose; Models, Molecular; Molecular Sequence Data; Protein Structure, Tertiary

1994
Maltal binding mechanism and a role of the mobile loop of soybean beta-amylase.
    Bioscience, biotechnology, and biochemistry, 1996, Volume: 60, Issue:7

    Topics: 1-Deoxynojirimycin; beta-Amylase; Binding Sites; Glycine max; Kinetics; Magnetic Resonance Spectroscopy; Maltose; Optical Rotation

1996
Anatomy of a conformational transition of beta-strand 6 in soybean beta-amylase caused by substrate (or inhibitor) binding to the catalytical site.
    Protein science : a publication of the Protein Society, 1997, Volume: 6, Issue:11

    Topics: alpha-Cyclodextrins; beta-Amylase; Binding Sites; Cyclodextrins; Glycine max; Maltose; Models, Molecular; Protein Structure, Secondary; Thermodynamics

1997