Page last updated: 2024-09-05

isochorismic acid and tryptophan

isochorismic acid has been researched along with tryptophan in 2 studies

Compound Research Comparison

Studies (isochorismic acid)	Trials (isochorismic acid)	Recent Studies (post-2010) (isochorismic acid)	Studies (tryptophan)	Trials (tryptophan)	Recent Studies (post-2010) (tryptophan)
52	0	18	32,762	936	7,183

Protein Interaction Comparison

Protein	Taxonomy	isochorismic acid (IC50)	tryptophan (IC50)
Myeloperoxidase	Homo sapiens (human)		2.25

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	1 (50.00)	29.6817
2010's	1 (50.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Kim, C; Mills, SE; Nguyen-Huu, X; Spraggon, G; Yanofsky, C; Yee, MC	1
Gulick, AM; Lamb, AL; Meneely, KM; Moran, GR; Sundlov, JA	1

Other Studies

2 other study(ies) available for isochorismic acid and tryptophan

Article	Year
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan. Proceedings of the National Academy of Sciences of the United States of America, 2001, May-22, Volume: 98, Issue:11 Topics: Amino Acid Sequence; Anthranilate Synthase; Base Sequence; Binding Sites; Chorismic Acid; Crystallography, X-Ray; Cyclohexenes; DNA, Bacterial; Glutamic Acid; Glutamine; Lyases; Molecular Sequence Data; Nitrogenous Group Transferases; Oligopeptides; ortho-Aminobenzoates; Protein Structure, Secondary; Serratia marcescens; Substrate Specificity; Tryptophan	2001
An Open and Shut Case: The Interaction of Magnesium with MST Enzymes. Journal of the American Chemical Society, 2016, 07-27, Volume: 138, Issue:29 Topics: Binding Sites; Catalytic Domain; Chorismic Acid; Intramolecular Transferases; Kinetics; Magnesium; Models, Molecular; Protein Binding; Siderophores; Tryptophan; Vitamin K 2	2016

Article

Year

The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.

Proceedings of the National Academy of Sciences of the United States of America, 2001, May-22, Volume: 98, Issue:11

Topics: Amino Acid Sequence; Anthranilate Synthase; Base Sequence; Binding Sites; Chorismic Acid; Crystallography, X-Ray; Cyclohexenes; DNA, Bacterial; Glutamic Acid; Glutamine; Lyases; Molecular Sequence Data; Nitrogenous Group Transferases; Oligopeptides; ortho-Aminobenzoates; Protein Structure, Secondary; Serratia marcescens; Substrate Specificity; Tryptophan

2001

An Open and Shut Case: The Interaction of Magnesium with MST Enzymes.

Journal of the American Chemical Society, 2016, 07-27, Volume: 138, Issue:29

Topics: Binding Sites; Catalytic Domain; Chorismic Acid; Intramolecular Transferases; Kinetics; Magnesium; Models, Molecular; Protein Binding; Siderophores; Tryptophan; Vitamin K 2

2016