EC Number |
Disease |
PubMed ID |
Title of Publication |
Category |
Confidence Level |
---|
2.3.3.13 | Starvation |
8045889 |
Regulation of tryptophan biosynthesis in Methanobacterium thermoautotrophicum Marburg. |
causal interaction unassigned |
4 0 |
2.3.3.13 | Tuberculosis |
15159590 |
Crystallization and preliminary X-ray analysis of alpha-isopropylmalate synthase from Mycobacterium tuberculosis. |
ongoing research unassigned |
3 0 |
2.3.3.13 | Tuberculosis |
16011356 |
Slow-onset feedback inhibition: inhibition of Mycobacterium tuberculosis alpha-isopropylmalate synthase by L-leucine. |
therapeutic application unassigned |
2 0 |
2.3.3.13 | Tuberculosis |
16684501 |
Kinetic analysis of the effects of monovalent cations and divalent metals on the activity of Mycobacterium tuberculosis alpha-isopropylmalate synthase. |
ongoing research unassigned |
3 0 |
2.3.3.13 | Tuberculosis |
16846242 |
Kinetic and chemical mechanism of alpha-isopropylmalate synthase from Mycobacterium tuberculosis. |
ongoing research unassigned |
3 0 |
2.3.3.13 | Tuberculosis |
17577419 |
Cation induced differential effect on structural and functional properties of Mycobacterium tuberculosis alpha-isopropylmalate synthase. |
causal interaction ongoing research therapeutic application unassigned |
3 3 4 0 |
2.3.3.13 | Tuberculosis |
18647358 |
The significance and effect of tandem repeats within the Mycobacterium tuberculosis leuA gene on alpha-isopropylmalate synthase. |
ongoing research unassigned |
2 0 |
2.3.3.13 | Tuberculosis |
19166329 |
Kinetic Evidence for Interdomain Communication in the Allosteric Regulation of alpha-Isopropylmalate Synthase from Mycobacterium tuberculosis (dagger). |
ongoing research unassigned |
2 0 |
2.3.3.13 | Tuberculosis |
19505340 |
Characterization of alpha-isopropylmalate synthases containing different copy numbers of tandem repeats in Mycobacterium tuberculosis. |
therapeutic application unassigned |
1 0 |
2.3.3.13 | Tuberculosis |
19606873 |
Mapping of the allosteric network in the regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis by the feedback inhibitor L-leucine: solution-phase H/D exchange monitored by FT-ICR mass spectrometry. |
ongoing research unassigned |
1 0 |