proline and 5-androstene-3,17-dione

proline has been researched along with 5-androstene-3,17-dione in 1 studies

Research

Studies (1)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Cha, SS; Choi, KY; Hong, BH; Lee, HS; Nam, GH; Oh, YH; Yun, YS	1

Other Studies

1 other study(ies) available for proline and 5-androstene-3,17-dione

Article	Year
The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni. The Biochemical journal, 2003, Oct-15, Volume: 375, Issue:Pt 2 Topics: Androstenedione; Aspartic Acid; Binding Sites; Catalysis; Catalytic Domain; Comamonas testosteroni; Conserved Sequence; Crystallography, X-Ray; Enzyme Stability; Equilenin; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Mutation; Proline; Protein Binding; Protein Folding; Protein Structure, Tertiary; Steroid Isomerases; Structure-Activity Relationship; Substrate Specificity; Thermodynamics	2003

Article

Year

The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni.

The Biochemical journal, 2003, Oct-15, Volume: 375, Issue:Pt 2

Topics: Androstenedione; Aspartic Acid; Binding Sites; Catalysis; Catalytic Domain; Comamonas testosteroni; Conserved Sequence; Crystallography, X-Ray; Enzyme Stability; Equilenin; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Mutation; Proline; Protein Binding; Protein Folding; Protein Structure, Tertiary; Steroid Isomerases; Structure-Activity Relationship; Substrate Specificity; Thermodynamics

2003