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Ribulose-5-Phosphate-3-Epimerase (RPE)

Ribulose-5-phosphate-3-epimerase catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.

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Ribulose-5-Phosphate-3-Epimerase (RPE) Related Products

Ribulose-5-Phosphate-3-Epimerase (RPE) Proteins

Ribulose-5-Phosphate-3-Epimerase (RPE) Antibodies

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Ribulose-5-Phosphate-3-Epimerase (RPE) ELISA Pair sets

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Ribulose-5-Phosphate-3-Epimerase (RPE) cDNA Clones

Ribulose-5-Phosphate-3-Epimerase (RPE) Related Areas

Enzyme>>Carbohydrate Metabolism Enzymes>>RPE

Ribulose-5-Phosphate-3-Epimerase (RPE) Related Pathways

Ribulose-5-Phosphate-3-Epimerase (RPE) Alternative Names

RPE, HUSSY-17, MGC2636, RPE2-1 [Homo sapiens]

Rpe, AC118589.1, 2810429B02Rik, 5730518J08Rik [Mus musculus]

Summaries for Ribulose-5-Phosphate-3-Epimerase (RPE)

Wikipedia summary for Ribulose-5-Phosphate-3-Epimerase (RPE):

In enzymology, a ribulose-phosphate 3-epimerase (also known as pentose-5-phosphate 3-epimerase or PPE) is the enzyme that converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle.
D-ribulose 5-phosphate = D-xylulose 5-phosphate
Hence, this enzyme has one substrate, D-ribulose 5-phosphate, and one product, D-xylulose 5-phosphate. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives.
In Alcaligenes eutrophus two copies of the gene coding for PPE are known , one is chromosomally encoded P40117, the other one is on a plasmid Q04539. PPE has been found in a wide range of bacteria, archaebacteria, fungi and plants. All the proteins have from 209 to 241 amino acid residues. The enzyme has a TIM barrel structure.
The systematic name of this enzyme class is D-ribulose-5-phosphate 3-epimerase. Other names in common use include phosphoribulose epimerase, erythrose-4-phosphate isomerase, phosphoketopentose 3-epimerase, xylulose phosphate 3-epimerase, phosphoketopentose epimerase, ribulose 5-phosphate 3-epimerase, D-ribulose phosphate-3-epimerase, D-ribulose 5-phosphate epimerase, D-ribulose-5-P 3-epimerase, D-xylulose-5-phosphate 3-epimerase, and pentose-5-phosphate 3-epimerase.
This enzyme participates in 3 metabolic pathways: pentose phosphate pathway, pentose and glucuronate interconversions, and carbon fixation.

Human Ribulose-5-Phosphate-3-Epimerase (RPE) Protein General Information

 

Protein names

Ribulose-5-Phosphate-3-Epimerase
Short name=RPE

Sequence length

228 AA.

Cofactor

Binds 1 divalent metal cation per subunit. Contains tightly bound Fe2+ when produced in E.coli, but the physiological cofactor may be Co2+, Mn2+ or Zn2+.

Sequence similarities:

Belongs to the ribulose-phosphate 3-epimerase family.

Catalytic activity:

D-ribulose 5-phosphate = D-xylulose 5-phosphate.

Subunit structure

Homodimer.

Sequence caution: The sequence BAB71076.1 differs from that shown. Reason: Frameshift at position 69.
The sequence BAC04212.1 differs from that shown. Reason: Frameshift at position 42.

General information above from UniProt

Function for Ribulose-5-Phosphate-3-Epimerase (RPE) Protein

UniProtKB:

Ribulose-5-phosphate-3-epimerase catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.

Genatlas:

  • Ribulose-5-phosphate-3-epimerase is involved in nonsense-mediated decay of mRNAs containing premature stop codons
  • Ribulose-5-phosphate-3-epimerase is required for the 3' processing of the 7s pre-RNA to the mature 5.8s rRNA

Homology for human Ribulose-5-Phosphate-3-Epimerase (RPE)

Phenotype Information for Ribulose-5-Phosphate-3-Epimerase (RPE)

Drugs for Ribulose-5-Phosphate-3-Epimerase (RPE)

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