Compounds > d-tagatose 1,6-diphosphate
Page last updated: 2024-09-05

d-tagatose 1,6-diphosphate and fructose-1,6-diphosphate

d-tagatose 1,6-diphosphate has been researched along with fructose-1,6-diphosphate in 4 studies

Compound Research Comparison

Studies
(d-tagatose 1,6-diphosphate)		Trials
(d-tagatose 1,6-diphosphate)		Recent Studies (post-2010)
(d-tagatose 1,6-diphosphate)		Studies
(fructose-1,6-diphosphate)		Trials
(fructose-1,6-diphosphate)		Recent Studies (post-2010) (fructose-1,6-diphosphate)
100289720149

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's4 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Berry, A; Qamar, S; Thomson, GJ; Zgiby, SM1
Berry, A; Domann, S; Nelson, A; Williams, GJ1
Bae, J; Choi, Y; Eom, SH; Hong, SI; Im, YJ; Kang, GB; Kim, D; Kim, JS; Kim, MK; Koh, S; Lee, DS; Lee, JH1
Dunaway-Mariano, D; Galkin, A; Herzberg, O; Kulakova, L; Li, L; Li, Z; Pal, LR1

Other Studies

4 other study(ies) available for d-tagatose 1,6-diphosphate and fructose-1,6-diphosphate

ArticleYear
Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases.
    European journal of biochemistry, 2000, Volume: 267, Issue:6

    Topics: Aldehyde-Lyases; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Binding Sites; Catalysis; Cloning, Molecular; Crystallography, X-Ray; Enzyme Induction; Escherichia coli; Fructose-Bisphosphate Aldolase; Fructosediphosphates; Hexosediphosphates; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Sequence Alignment; Sequence Homology, Amino Acid; Stereoisomerism; Substrate Specificity

2000
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution.
    Proceedings of the National Academy of Sciences of the United States of America, 2003, Mar-18, Volume: 100, Issue:6

    Topics: Aldehyde-Lyases; Catalytic Domain; Directed Molecular Evolution; Escherichia coli; Fructosediphosphates; Hexosediphosphates; Kinetics; Models, Molecular; Mutation; Nuclear Magnetic Resonance, Biomolecular; Recombinant Proteins; Stereoisomerism; Substrate Specificity

2003
Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus.
    Biochemical and biophysical research communications, 2006, Sep-01, Volume: 347, Issue:3

    Topics: Binding Sites; Crystallography, X-Ray; Fructose-Bisphosphate Aldolase; Fructosediphosphates; Hexosediphosphates; Models, Molecular; Molecular Sequence Data; Protein Structure, Quaternary; Protein Structure, Tertiary; Receptors, Amino Acid; Sequence Alignment; Stereoisomerism; Structural Homology, Protein; Substrate Specificity; Thermus

2006
Structural insights into the substrate binding and stereoselectivity of giardia fructose-1,6-bisphosphate aldolase.
    Biochemistry, 2009, Apr-14, Volume: 48, Issue:14

    Topics: Animals; Catalytic Domain; Crystallography, X-Ray; Fructose-Bisphosphate Aldolase; Fructosediphosphates; Giardia; Hexosediphosphates; Kinetics; Protein Binding; Protein Conformation; Protozoan Proteins; Stereoisomerism; Substrate Specificity; Zinc

2009