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Literature summary for 1.8.4.10 extracted from
- Noncovalent Complexes of APS Reductase from M. tuberculosis: Delineating a Mechanistic Model Using ESI-FTICR MS (2007), J. Am. Soc. Mass Spectrom., 18, 167-178.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | 4Fe-4S containing protein. Oxidation state of +2 for the 4Fe-4S cluster, with no disulfide bond in the holoenzyme | Mycobacterium tuberculosis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | - |
recombinantly expressed in Escherichia coli | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| adenosine 5'-phosphosulfate + thioredoxin | noncovalent complexes of the holoprotein with several ligands, including adenosine 5'-phosphosulfate, thioredoxin, and AMP, are investigated. AMP binds with a higher affinity to the enzyme intermediate than to the free enzyme | Mycobacterium tuberculosis | AMP + sulfite + thioredoxin disulfide | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| APS reductase | - |
Mycobacterium tuberculosis |
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Release 2023.1 (January 2023)
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