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Literature summary for 1.13.11.54 extracted from

  • Dai, Y.; Wensink, P.C.; Abeles, R.H.
    One protein, two enzymes (1999), J. Biol. Chem., 274, 1193-1195.
    View publication on PubMed
Search for more literature for 1.13.11.54

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Klebsiella oxytoca

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
210
-
 O2
-
 Klebsiella oxytoca
210
-
 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one
-
 Klebsiella oxytoca

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ apoenzyme is catalytically inactive. Addition of Fe2+ yields activity. Production of the enzyme in intact Escherichia coli depends on the availability of the Fe2+. Enzyme contains 0.9 Fe2+ per enzyme molecule Klebsiella oxytoca

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
20240
-
 mass spectrometry Klebsiella oxytoca

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 oxytoca enzyme of the methionine salvage pathway 4-(methylthio)-2-oxobutanoate + formate
-
 ?

Organism

Organism UniProt Comment Textmining
Klebsiella oxytoca Q9ZFE7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Klebsiella oxytoca

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 enzyme of the methionine salvage pathway Klebsiella oxytoca 4-(methylthio)-2-oxobutanoate + formate
-
 ?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 Fe2+ bound to the enzyme protein. If Ni2+ or Co2+ is bound instead of Fe+, the reaction catalzed by EC 1.13.11.53 occurs instead Klebsiella oxytoca 4-(methylthio)-2-oxobutanoate + formate
-
 ?