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Literature summary for 5.1.3.1 extracted from

  • Sobota, J.M.; Imlay, J.A.
    Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese (2011), Proc. Natl. Acad. Sci. USA, 108, 5402-5407.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Co2+ is able to activate the enzyme in vitro Escherichia coli
Fe2+ the enzyme employs a ferrous iron atom as a solvent-exposed cofactor Escherichia coli
Mn2+ manganese can activate the enzyme in vitro in place of iron converting the enzyme to a form that is unaffected by H2O2 Escherichia coli
additional information Ca2+, Cd2+, Cu2+, Mg2+, and Ni2+ do not activate the enzyme Escherichia coli
Zn2+ Zn2+ is able to activate the enzyme in vitro Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Oxidation Stability

Oxidation Stability Organism
ribulose-5-phosphate 3-epimerase is vulnerable to H2O2 damage in vivo. H2O2 rapidly oxidizes the Fe2+ in a Fenton reaction, the oxidized iron is released immediately, causing a loss of activity. When purified enzyme is loaded with Mn2+, Co2+, or Zn2+, there is no loss in activity when challenged with H2O2 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Ribulose 5-phosphate
-
Escherichia coli D-Xylulose 5-phosphate
-
r

Synonyms

Synonyms Comment Organism
ribulose-5-phosphate 3-epimerase
-
Escherichia coli
RPE
-
Escherichia coli