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n-acetylglutamic acid and alpha-chymotrypsin

n-acetylglutamic acid has been researched along with alpha-chymotrypsin 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
Bendala, E; Britton, HG; Cervera, J; Lusty, CJ; Rubio, V	1
Bagonis, M; Claridge, TD; Clifton, IJ; Domene, C; Iqbal, A; Kershaw, NJ; Schofield, CJ; Wharton, CW	1

Other Studies

2 other study(ies) available for n-acetylglutamic acid and alpha-chymotrypsin

Article	Year
Domain structure of the large subunit of Escherichia coli carbamoyl phosphate synthetase. Location of the binding site for the allosteric inhibitor UMP in the COOH-terminal domain. Biochemistry, 1991, Jan-29, Volume: 30, Issue:4 Topics: Adenosine Triphosphate; Affinity Labels; Allosteric Regulation; Binding Sites; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Chymotrypsin; Escherichia coli; Glutamates; Hydrolysis; Inosine Monophosphate; Ornithine; Pancreatic Elastase; Protein Conformation; Serine Endopeptidases; Trypsin; Uridine Monophosphate	1991
Anatomy of a simple acyl intermediate in enzyme catalysis: combined biophysical and modeling studies on ornithine acetyl transferase. Journal of the American Chemical Society, 2009, Jan-21, Volume: 131, Issue:2 Topics: Acetyltransferases; Acylation; Catalysis; Chymotrypsin; Computer Simulation; Crystallography, X-Ray; Glutamates; Models, Chemical; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Phenylpropionates; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry, Infrared	2009

Article

Year

Domain structure of the large subunit of Escherichia coli carbamoyl phosphate synthetase. Location of the binding site for the allosteric inhibitor UMP in the COOH-terminal domain.

Biochemistry, 1991, Jan-29, Volume: 30, Issue:4

Topics: Adenosine Triphosphate; Affinity Labels; Allosteric Regulation; Binding Sites; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Chymotrypsin; Escherichia coli; Glutamates; Hydrolysis; Inosine Monophosphate; Ornithine; Pancreatic Elastase; Protein Conformation; Serine Endopeptidases; Trypsin; Uridine Monophosphate

1991

Anatomy of a simple acyl intermediate in enzyme catalysis: combined biophysical and modeling studies on ornithine acetyl transferase.

Journal of the American Chemical Society, 2009, Jan-21, Volume: 131, Issue:2

Topics: Acetyltransferases; Acylation; Catalysis; Chymotrypsin; Computer Simulation; Crystallography, X-Ray; Glutamates; Models, Chemical; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Phenylpropionates; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry, Infrared

2009