glutamic acid and isomaltose

glutamic acid has been researched along with isomaltose in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	2 (100.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Ford, C; Reilly, PJ; Sierks, MR; Svensson, B	1
Clarke, AJ; Fierobe, HP; Svensson, B; Tull, D	1

Other Studies

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

Article	Year
Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori. Protein engineering, 1990, Volume: 3, Issue:3 Topics: Amino Acid Sequence; Aspartic Acid; Aspergillus; Base Sequence; Binding Sites; Catalysis; DNA Restriction Enzymes; Glucan 1,4-alpha-Glucosidase; Glucans; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Isomaltose; Kinetics; Maltose; Molecular Sequence Data; Mutation; Sequence Homology, Nucleic Acid; Structure-Activity Relationship; Thermodynamics	1990
Enzymatic properties of the cysteinesulfinic acid derivative of the catalytic-base mutant Glu400-->Cys of glucoamylase from Aspergillus awamori. Biochemistry, 1998, Mar-17, Volume: 37, Issue:11 Topics: 1-Deoxynojirimycin; Acarbose; Amino Acid Substitution; Amino Sugars; Aspergillus; Binding, Competitive; Catalysis; Cysteine; Enzyme Activation; Glucan 1,4-alpha-Glucosidase; Glucose; Glutamic Acid; Hydro-Lyases; Hydrogen-Ion Concentration; Hydrolysis; Isomaltose; Kinetics; Magnetic Resonance Spectroscopy; Mutation; Neurotransmitter Agents; Oligosaccharides; Polysaccharides; Trisaccharides	1998

Article

Year

Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.

Protein engineering, 1990, Volume: 3, Issue:3

Topics: Amino Acid Sequence; Aspartic Acid; Aspergillus; Base Sequence; Binding Sites; Catalysis; DNA Restriction Enzymes; Glucan 1,4-alpha-Glucosidase; Glucans; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Isomaltose; Kinetics; Maltose; Molecular Sequence Data; Mutation; Sequence Homology, Nucleic Acid; Structure-Activity Relationship; Thermodynamics

1990

Enzymatic properties of the cysteinesulfinic acid derivative of the catalytic-base mutant Glu400-->Cys of glucoamylase from Aspergillus awamori.

Biochemistry, 1998, Mar-17, Volume: 37, Issue:11

Topics: 1-Deoxynojirimycin; Acarbose; Amino Acid Substitution; Amino Sugars; Aspergillus; Binding, Competitive; Catalysis; Cysteine; Enzyme Activation; Glucan 1,4-alpha-Glucosidase; Glucose; Glutamic Acid; Hydro-Lyases; Hydrogen-Ion Concentration; Hydrolysis; Isomaltose; Kinetics; Magnetic Resonance Spectroscopy; Mutation; Neurotransmitter Agents; Oligosaccharides; Polysaccharides; Trisaccharides

1998