enterobactin has been researched along with tryptophan in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (33.33) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 2 (66.67) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Gaffney, T; Gong, F; Lam, S; Pierson, LS | 1 |
| Ma, L; Payne, SM | 1 |
| Campbell, C; Foshag, D; Pawelek, PD | 1 |
3 other study(ies) available for enterobactin and tryptophan
| Article | Year |
|---|---|
Molecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium. Pseudomonas aureofaciens 30-84.
Topics: Amino Acid Sequence; Anthranilate Synthase; Anti-Bacterial Agents; Bacterial Proteins; DNA, Bacterial; Enterobactin; Escherichia coli; Genes, Bacterial; Molecular Sequence Data; Open Reading Frames; Phenazines; Pseudomonas; Restriction Mapping; Sequence Homology, Amino Acid; Shikimic Acid; Tryptophan | 1995 |
AhpC is required for optimal production of enterobactin by Escherichia coli.
Topics: Chorismic Acid; Culture Media; Enterobactin; Escherichia coli; Escherichia coli Proteins; Gene Deletion; Hydroxybenzoates; Iron; para-Aminobenzoates; Peroxiredoxins; Phenylalanine; Shikimic Acid; Tryptophan; Tyrosine | 2012 |
The C-glycosyltransferase IroB from pathogenic Escherichia coli: identification of residues required for efficient catalysis.
Topics: Amino Acid Sequence; Amino Acid Substitution; Aspartic Acid; Biocatalysis; Catalytic Domain; Enterobactin; Escherichia coli Proteins; Glucosyltransferases; Glutamic Acid; Glycosylation; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Sequence Alignment; Siderophores; Structural Homology, Protein; Tryptophan; Uridine Diphosphate Glucose; Uropathogenic Escherichia coli | 2014 |