Page last updated: 2024-08-17

aspartic acid and maltoheptaose

aspartic acid has been researched along with maltoheptaose 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
Ford, C; Reilly, PJ; Sierks, MR; Svensson, B	1
Christensen, T; Frandsen, TP; Kaarsholm, NC; Sigurskjold, BW; Svensson, B	1

Other Studies

2 other study(ies) available for aspartic acid and maltoheptaose

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
Physicochemical characterisation of the two active site mutants Trp(52)-->Phe and Asp(55)-->Val of glucoamylase from Aspergillus niger. Biochimica et biophysica acta, 2002, Dec-16, Volume: 1601, Issue:2 Topics: Amino Acid Substitution; Aspartic Acid; Aspergillus niger; Binding Sites; Calorimetry; Glucan 1,4-alpha-Glucosidase; Glucans; Guanidine; Kinetics; Maltose; Mutation; Phenylalanine; Protein Conformation; Protein Denaturation; Sequence Deletion; Substrate Specificity; Tryptophan; Valine	2002

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

Physicochemical characterisation of the two active site mutants Trp(52)-->Phe and Asp(55)-->Val of glucoamylase from Aspergillus niger.

Biochimica et biophysica acta, 2002, Dec-16, Volume: 1601, Issue:2

Topics: Amino Acid Substitution; Aspartic Acid; Aspergillus niger; Binding Sites; Calorimetry; Glucan 1,4-alpha-Glucosidase; Glucans; Guanidine; Kinetics; Maltose; Mutation; Phenylalanine; Protein Conformation; Protein Denaturation; Sequence Deletion; Substrate Specificity; Tryptophan; Valine

2002