Compounds > nitrophenylgalactosides
Page last updated: 2024-08-26

nitrophenylgalactosides and glutamic acid

nitrophenylgalactosides has been researched along with glutamic acid in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (80.00)18.2507
2000's1 (20.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Aebersold, R; Gebler, JC; Withers, SG1
Cupples, CG; Huber, RE; Miller, JH1
Amyes, TL; Heo, C; Huber, RE; Lin, S; Richard, JP1
Kaback, HR; Kharabi, D; le Coutre, J; le Maire, G; Lee, JC; Sahin-Tóth, M1
Kaback, HR; Sahin-Toth, M1

Other Studies

5 other study(ies) available for nitrophenylgalactosides and glutamic acid

ArticleYear
Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli.
    The Journal of biological chemistry, 1992, Jun-05, Volume: 267, Issue:16

    Topics: Amino Acid Sequence; beta-Galactosidase; Binding Sites; Catalysis; Enzyme Activation; Escherichia coli; Fucose; Glutamates; Glutamic Acid; Glycosides; Kinetics; Molecular Sequence Data; Nitrophenylgalactosides

1992
Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis.
    The Journal of biological chemistry, 1990, Apr-05, Volume: 265, Issue:10

    Topics: beta-Galactosidase; Binding Sites; Drug Stability; Edetic Acid; Escherichia coli; Galactosidases; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Kinetics; Lactose; Mutation; Nitrophenylgalactosides; Ribose; Structure-Activity Relationship

1990
Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 3. Evidence that Glu-461 participates in Brønsted acid-base catalysis of beta-D-galactopyranosyl group transfer.
    Biochemistry, 1996, Sep-24, Volume: 35, Issue:38

    Topics: Azides; beta-Galactosidase; Catalysis; Escherichia coli; Galactose; Galactosides; Glutamic Acid; Kinetics; Magnesium; Mutation; Nitrophenylgalactosides; Structure-Activity Relationship; Trifluoroethanol

1996
Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli.
    Biochemistry, 1999, Jan-12, Volume: 38, Issue:2

    Topics: Amino Acid Substitution; Arginine; Binding Sites; Biological Transport, Active; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Glutamic Acid; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protons; Substrate Specificity; Symporters; Thiogalactosides

1999
Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichiacoli.
    Proceedings of the National Academy of Sciences of the United States of America, 2001, May-22, Volume: 98, Issue:11

    Topics: Arginine; Biological Transport; Biological Transport, Active; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis; Nitrophenylgalactosides; Protons; Substrate Specificity; Symporters

2001