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Literature summary for 1.13.11.53 extracted from

  • Pochapsky, T.C.; Pochapsky, S.S.; Ju, T.; Mo, H.; Al-Mjeni, F.; Maroney, M.J.
    Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae (2002), Nat. Struct. Biol., 9, 966-972.
    View publication on PubMed

Metals/Ions

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/ Products (Substrates)

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
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Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
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Klebsiella pneumoniae 3-(methylthio)propanoate + formate + CO
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?
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
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?

Synonyms

Synonyms Comment Organism
ARD
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Klebsiella pneumoniae