Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ni2+ | solution structure of the nickel-containing enzyme is determined using NMR methods. X-ray absorption spectroscopy, assignment of hyperfine shifted NMR resonance and conserved domain homology are used to model the metal-binding site because of the paramagnetism of the bound Ni2+ | Klebsiella pneumoniae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 | Klebsiella pneumoniae | the enzyme represents a branch point in the methionine salvage pathway leading from methylthioadenosine to methionine | 3-(methylthio)propanoate + formate + CO | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella pneumoniae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 | - |
Klebsiella pneumoniae | 3-(methylthio)propanoate + formate + CO | - |
? | |
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 | the enzyme represents a branch point in the methionine salvage pathway leading from methylthioadenosine to methionine | Klebsiella pneumoniae | 3-(methylthio)propanoate + formate + CO | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ARD | - |
Klebsiella pneumoniae |