5.1.3.4: L-ribulose-5-phosphate 4-epimerase
This is an abbreviated version!
For detailed information about L-ribulose-5-phosphate 4-epimerase, go to the full flat file.
Word Map on EC 5.1.3.4
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5.1.3.4
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l-fuculose-1-phosphate
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l-arabinose
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epimerization
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l-ribulokinase
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dihydroxyacetone
-
arabad
-
aldol
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glycolaldehyde
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aldolases
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typhimurium
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sphere
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d-glucose
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flip
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ara
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enolate
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aerogenes
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carbon-carbon
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stereocenter
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aerobacter
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l-rhamnulose-1-phosphate
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aldolase-like
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synthesis
- 5.1.3.4
- l-fuculose-1-phosphate
- l-arabinose
-
epimerization
- l-ribulokinase
- dihydroxyacetone
-
arabad
-
aldol
- glycolaldehyde
- aldolases
- typhimurium
-
sphere
- d-glucose
- flip
-
ara
-
enolate
- aerogenes
-
carbon-carbon
-
stereocenter
-
aerobacter
- l-rhamnulose-1-phosphate
-
aldolase-like
- synthesis
Reaction
Synonyms
araD, Epimerase, L-ribulose phosphate 4-, L-Ribulose phosphate 4-epimerase, L-Ribulose-5-phosphate 4-epimerase, Phosphoribulose isomerase, Ribulose phosphate 4-epimerase
ECTree
5.1.3.4 L-ribulose-5-phosphate 4-epimeraseAdvanced search results
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results (Metals Ions
Metals Ions on EC 5.1.3.4 - L-ribulose-5-phosphate 4-epimerase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
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divalent metal ion required. Reactivated by addition of divalent metal ion in decreasing order: Mn2+, Co2+, Ni2+, Ca2+, Zn2+, Mg2+
Co2+
Cu2+
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the enzyme preparation contains a mixture of the following metals in order of decreasing abundance: Zn2+, Mn2+, Cu2+
Mg2+
Mn2+
Ni2+
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divalent metal ion required. Reactivated by addition of divalent metal ion in decreasing order: Mn2+, Co2+, Ni2+, Ca2+, Zn2+, Mg2+
Zinc
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the catalytic zinc residue is located at the interface between two adjacent subunits
Zn2+
Co2+
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can replace Zn2+ in mutant enzyme Y229F and in wild-type enzyme, Km-value for wild-type enzyme is 0.00029 mM
Co2+
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divalent metal ion required. Reactivated by addition of divalent metal ion in decreasing order: Mn2+, Co2+, Ni2+, Ca2+, Zn2+, Mg2+
Mg2+
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poorly bound, weak activator, KM-value for wild-type enzyme is 1.35 mM
Mg2+
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divalent metal ion required. Reactivated by addition of divalent metal ion in decreasing order: Mn2+, Co2+, Ni2+, Ca2+, Zn2+, Mg2+
Mn2+
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can replace Zn2+ in mutant enzyme Y229F and in wild-type enzyme. Km-value for wild-type enzyme is 0.00054 mM
Mn2+
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the enzyme preparation contains a mixture of the following metals in order of decreasing abundance: Zn2+, Mn2+, Cu2+
Mn2+
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reactivated after EDTA treatment by addition of divalent metal ion in decreasing order: Mn2+, Co2+, Ni2+, Ca2+, Zn2+, Mg2+
Mn2+
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in presence of the optimal concentration of Mn2+ the specific activity is 5times greater than that displayed by the crystalline enzyme as isolated and assayed in absence of added metal
Zn2+
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H95N, H97N, and D76N mutant enzymes require exogenous metal ions for full activity
Zn2+
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the enzyme preparation contains a mixture of the following metals in order of decreasing abundance: Zn2+, Mn2+, Cu2+
Zn2+
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divalent metal ion required. Reactivated by addition of divalent metal ion in decreasing order: Mn2+, Co2+, Ni2+, Ca2+, Zn2+, Mg2+
