serine and beta-isopropylmalate

serine has been researched along with beta-isopropylmalate in 2 studies

Research

Studies (2)

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

Authors

Authors	Studies
Doyle, SA; Fung, SY; Koshland, DE	1
Beernink, PT; Doyle, SA; Koshland, DE	1

Other Studies

2 other study(ies) available for serine and beta-isopropylmalate

Article	Year
Redesigning the substrate specificity of an enzyme: isocitrate dehydrogenase. Biochemistry, 2000, Nov-21, Volume: 39, Issue:46 Topics: 3-Isopropylmalate Dehydrogenase; Alcohol Oxidoreductases; Amino Acid Sequence; Amino Acid Substitution; Asparagine; Enzyme Activation; Escherichia coli; Glutamic Acid; Helix-Loop-Helix Motifs; Isocitrate Dehydrogenase; Isocitrates; Malates; Molecular Sequence Data; Mutagenesis, Insertional; Mutagenesis, Site-Directed; Protein Engineering; Protein Structure, Secondary; Recombinant Fusion Proteins; Serine; Substrate Specificity; Thermus thermophilus; Thiobacillus; Valine	2000
Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP. Biochemistry, 2001, Apr-10, Volume: 40, Issue:14 Topics: Amino Acid Substitution; Binding Sites; Catalysis; Crystallography, X-Ray; Escherichia coli; Freezing; Glutamic Acid; Isocitrate Dehydrogenase; Macromolecular Substances; Magnesium; Malates; NADP; Protein Structure, Secondary; Protein Structure, Tertiary; Serine; Structure-Activity Relationship; Substrate Specificity; Tyrosine	2001

Article

Year

Redesigning the substrate specificity of an enzyme: isocitrate dehydrogenase.

Biochemistry, 2000, Nov-21, Volume: 39, Issue:46

Topics: 3-Isopropylmalate Dehydrogenase; Alcohol Oxidoreductases; Amino Acid Sequence; Amino Acid Substitution; Asparagine; Enzyme Activation; Escherichia coli; Glutamic Acid; Helix-Loop-Helix Motifs; Isocitrate Dehydrogenase; Isocitrates; Malates; Molecular Sequence Data; Mutagenesis, Insertional; Mutagenesis, Site-Directed; Protein Engineering; Protein Structure, Secondary; Recombinant Fusion Proteins; Serine; Substrate Specificity; Thermus thermophilus; Thiobacillus; Valine

2000

Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP.

Biochemistry, 2001, Apr-10, Volume: 40, Issue:14

Topics: Amino Acid Substitution; Binding Sites; Catalysis; Crystallography, X-Ray; Escherichia coli; Freezing; Glutamic Acid; Isocitrate Dehydrogenase; Macromolecular Substances; Magnesium; Malates; NADP; Protein Structure, Secondary; Protein Structure, Tertiary; Serine; Structure-Activity Relationship; Substrate Specificity; Tyrosine

2001