asparagine and phosphoenolpyruvate

asparagine has been researched along with phosphoenolpyruvate 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
Amrhein, N; Etezady-Esfarjani, T; Macheroux, P; Samland, AK	1
Gatti, DL; Kona, F; Kuzmic, P; Martin, P; Xu, X	1

Other Studies

2 other study(ies) available for asparagine and phosphoenolpyruvate

Article	Year
Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae. Biochemistry, 2001, Feb-13, Volume: 40, Issue:6 Topics: Alkyl and Aryl Transferases; Amino Acid Substitution; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Cysteine; Enterobacter cloacae; Enzyme Inhibitors; Fosfomycin; Mutagenesis, Site-Directed; Phosphates; Phosphoenolpyruvate; Recombinant Proteins; Uridine Diphosphate N-Acetylglucosamine	2001
Structural and mechanistic changes along an engineered path from metallo to nonmetallo 3-deoxy-D-manno-octulosonate 8-phosphate synthases. Biochemistry, 2007, Apr-17, Volume: 46, Issue:15 Topics: Aldehyde-Lyases; Asparagine; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Cysteine; Enzyme Stability; Kinetics; Metals; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Phosphoenolpyruvate; Protein Binding; Substrate Specificity	2007

Article

Year

Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae.

Biochemistry, 2001, Feb-13, Volume: 40, Issue:6

Topics: Alkyl and Aryl Transferases; Amino Acid Substitution; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Cysteine; Enterobacter cloacae; Enzyme Inhibitors; Fosfomycin; Mutagenesis, Site-Directed; Phosphates; Phosphoenolpyruvate; Recombinant Proteins; Uridine Diphosphate N-Acetylglucosamine

2001

Structural and mechanistic changes along an engineered path from metallo to nonmetallo 3-deoxy-D-manno-octulosonate 8-phosphate synthases.

Biochemistry, 2007, Apr-17, Volume: 46, Issue:15

Topics: Aldehyde-Lyases; Asparagine; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Cysteine; Enzyme Stability; Kinetics; Metals; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Phosphoenolpyruvate; Protein Binding; Substrate Specificity

2007