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Literature summary for 2.8.1.7 extracted from
- The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli (2003), J. Biol. Chem., 278, 45713-45719.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Suf protein family | SufE protein can stimulate up to 8fold, addition of the SufBCD complex further stimulates up to 32fold | Escherichia coli | |
| SufE | SufE protein can stimulate up to 8fold | Escherichia coli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-cysteine + [enzyme]-cysteine | Escherichia coli | - |
L-alanine + [enzyme]-S-sulfanylcysteine | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.008 | - |
recombinant enzyme with L-cysteine as substrate | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-cysteine + [enzyme]-cysteine | - |
Escherichia coli | L-alanine + [enzyme]-S-sulfanylcysteine | - |
? | |
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