Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | inhibitor binding structure, binding energies, dissociation constants, and inhibition mechanisms, overview | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | the enzyme contains a [4Fe-4S] cluster cofactor | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenylyl sulfate + cofactor sulfide | Mycobacterium tuberculosis | the enzyme catalyzes the first committed step in bacterial sulfate reduction | AMP + sulfite + cofactor disulfide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
gene cysH | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenylyl sulfate + cofactor sulfide | the enzyme catalyzes the first committed step in bacterial sulfate reduction | Mycobacterium tuberculosis | AMP + sulfite + cofactor disulfide | - |
? | |
adenylyl sulfate + cofactor sulfide | conserved and semiconserved residues participate in four main-chain hydrogen bonds with adenine and the ribose O2'-hydroxyl, interaction between the phosphosulfate and APSR occurs via strictly conserved residues K144, R242, and R245, the phosphosulfate is also positioned opposite an [4Fe-4S] cofactor and Cys140. However, the substrate is not in direct contact with the [4Fe-4S] cluster, overview | Mycobacterium tuberculosis | AMP + sulfite + cofactor disulfide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
adenosine 5'-phosphosulfate reductase | - |
Mycobacterium tuberculosis |
APSR | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme contains a [4Fe-4S] cluster cofactor | Mycobacterium tuberculosis |