EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.4 | D-cycloserine | interferes with the formation of peptidoglycan biosynthesis by competitive inhibition of alanine racemase and D-alanine-D-alanine ligase, the latter is the primary lethal target, inhibition mechanism and physiological effects, NMR metabolomic study, overview. D-Alanine is able to effectively compete with the inhibitor for uptake | Mycobacterium tuberculosis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.4 | Mg2+ | required | Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.2.4 | ATP + 2 D-alanine | Mycobacterium tuberculosis | - |
ADP + phosphate + D-alanyl-D-alanine | - |
? | |
6.3.2.4 | ATP + 2 D-alanine | Mycobacterium tuberculosis H37Rv | - |
ADP + phosphate + D-alanyl-D-alanine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.2.4 | Mycobacterium tuberculosis | - |
- |
- |
6.3.2.4 | Mycobacterium tuberculosis H37Rv | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.2.4 | ATP + 2 D-alanine | - |
Mycobacterium tuberculosis | ADP + phosphate + D-alanyl-D-alanine | - |
? | |
6.3.2.4 | ATP + 2 D-alanine | - |
Mycobacterium tuberculosis H37Rv | ADP + phosphate + D-alanyl-D-alanine | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.4 | ATP | - |
Mycobacterium tuberculosis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.3.2.4 | additional information | NMR ligand binding assay for D-alanine-D-alanine ligase, overview | Mycobacterium tuberculosis |