Page last updated: 2024-08-25

pyruvamide and glutamic acid

pyruvamide has been researched along with glutamic acid in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Hübner, G; Kern, D; Kern, G; Killenberg-Jabs, M; Neef, H; Schneider, G; Tittmann, K; Wikner, C	1
Jordan, F; Sergienko, EA	1

Other Studies

2 other study(ies) available for pyruvamide and glutamic acid

Article	Year
How thiamine diphosphate is activated in enzymes. Science (New York, N.Y.), 1997, Jan-03, Volume: 275, Issue:5296 Topics: Allosteric Regulation; Binding Sites; Catalysis; Deuterium; Enzyme Activation; Glutamic Acid; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Protons; Pyruvate Decarboxylase; Pyruvates; Thermodynamics; Thiamine Pyrophosphate; Transketolase	1997
Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values. Biochemistry, 2001, Jun-26, Volume: 40, Issue:25 Topics: Acetaldehyde; Alanine; Amino Acid Substitution; Asparagine; Aspartic Acid; Binding Sites; Catalytic Domain; Computer Simulation; Glutamic Acid; Glutamine; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Pyruvate Decarboxylase; Pyruvates; Recombinant Proteins; Saccharomyces cerevisiae; Substrate Specificity	2001

Article

Year

How thiamine diphosphate is activated in enzymes.

Science (New York, N.Y.), 1997, Jan-03, Volume: 275, Issue:5296

Topics: Allosteric Regulation; Binding Sites; Catalysis; Deuterium; Enzyme Activation; Glutamic Acid; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Protons; Pyruvate Decarboxylase; Pyruvates; Thermodynamics; Thiamine Pyrophosphate; Transketolase

1997

Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values.

Biochemistry, 2001, Jun-26, Volume: 40, Issue:25

Topics: Acetaldehyde; Alanine; Amino Acid Substitution; Asparagine; Aspartic Acid; Binding Sites; Catalytic Domain; Computer Simulation; Glutamic Acid; Glutamine; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Pyruvate Decarboxylase; Pyruvates; Recombinant Proteins; Saccharomyces cerevisiae; Substrate Specificity

2001