EC Number   |
Disease |
PubMed ID |
Title of Publication |
Category |
Confidence Level |
|---|
    2.1.3.15 | Tuberculosis |
16492739 |
Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis. |
therapeutic application
unassigned |
2
0 |
| 2.1.3.15 | Tuberculosis |
17114269 |
AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis. |
diagnostic usage
ongoing research
unassigned |
3
2
0 |
| 2.1.3.15 | Tuberculosis |
17157300 |
Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis. |
causal interaction
diagnostic usage
therapeutic application
unassigned |
1
1
1
0 |
| 2.1.3.15 | Tuberculosis |
21984794 |
AccD6, a key carboxyltransferase essential for mycolic acid synthesis in Mycobacterium tuberculosis, is dispensable in a nonpathogenic strain. |
causal interaction
therapeutic application
unassigned |
1
4
0 |
| 2.1.3.15 | Tuberculosis |
22125378 |
Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis. |
ongoing research
unassigned |
2
0 |
| 2.1.3.15 | Tuberculosis |
24950047 |
Pleiotropic effect of AccD5 and AccE5 depletion in acyl-coenzyme A carboxylase activity and in lipid biosynthesis in mycobacteria. |
unassigned |
0 |
| 2.1.3.15 | Tuberculosis |
25092705 |
Structure, activity, and inhibition of the Carboxyltransferase ?-subunit of acetyl coenzyme A carboxylase (AccD6) from Mycobacterium tuberculosis. |
ongoing research
therapeutic application
unassigned |
1
2
0 |
