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Literature summary for 1.13.11.54 extracted from

  • Deshpande, A.R.; Pochapsky, T.C.; Petsko, G.A.; Ringe, D.
    Dual chemistry catalyzed by human acireductone dioxygenase (2017), Protein Eng. Des. Sel., 30, 197-204 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ Fe2+-form of enzyme, less than 1 mol per mol of protein Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9BV57
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2 i.e. desthio-acireductone Homo sapiens 2-oxovalerate + formic acid
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additional information human ARD is capable of metal-dependent dual chemistry. The Fe2+-bound ARD shows the highest activity and catalyzes on-pathway chemistry, i.e. reaction of EC 1.13.11.54, whereas Ni2+, Co2+ or Mn2+ forms catalyze off-pathway chemistry, i.e. reasctions of EC 1.13.11.53. The enzymatic activity is metal ion cofactor dependent and the activity trend in decreasing order is Fe2+ > Ni2+ = Co2+ > Mn2+ Homo sapiens ?
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Synonyms

Synonyms Comment Organism
ADI1
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Homo sapiens
ARD
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Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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Ni2+-bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable Homo sapiens