Phosphopentose epimerase
ribulose-phosphate 3-epimerase | |||||||||
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ExPASy NiceZyme view | | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Ribulose-phosphate 3 epimerase family | |||||||||||
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Identifiers | |||||||||||
Symbol | Ribul_P_3_epim | ||||||||||
SCOP2 | 1rpx / SCOPe / SUPFAM | ||||||||||
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Phosphopentose epimerase (also known as ribulose-phosphate 3-epimerase and ribulose 5-phosphate 3-epimerase, EC 5.1.3.1) encoded by the RPE gene is a metalloprotein that catalyzes the interconversion between D-ribulose 5-phosphate and D-xylulose 5-phosphate.[1]
- D-ribulose 5-phosphate D-xylulose 5-phosphate
This reversible conversion is required for
In Cupriavidus metallidurans two copies of the gene coding for PPE are known,[4] 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.
Nomenclature
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
The human protein containing this domain is the RPE (gene).
Family
Phosphopentose epimerase belongs to two protein families of increasing hierarchy. This enzyme belongs to the
Structure
As of late 2007, 4
Overall
Crystallographic studies have helped elucidate the
As previously mentioned, Phosphopentose epimerase is a metalloenzyme. It requires a
Active site
The β6/α6 loop region interacts with the substrate and regulates access to the active site. Phe147, Gly148, and Ala149 of this region cap the active site once binding has occurred. In addition, the Fe2+ ion is coordinated to His35, His70, Asp37, Asp175, and oxygens O2 and O3 of the substrate.
Mechanism
Phosphopentose utilizes an acid/base type of catalytic mechanism. The reaction proceeds in such a way that trans-2,3-enediol phosphate is the intermediate.
Function
Calvin cycle
Pentose phosphate pathway
The reactions of the pentose phosphate pathway (PPP) take place in the cytoplasm. Phosphopentose epimerase specifically affects the nonoxidative portion of the pathway, which involves the production of various sugars and precursors.[2] This enzyme converts ribulose 5-phosphate into the appropriate epimer for the transketolase reaction, xylulose 5-phosphate.[11] Therefore, the reaction that occurs in the pentose phosphate pathway is exactly the reverse of the reaction which occurs in the Calvin cycle. The mechanism remains the same and involves the formation of an enediolate intermediate.
Due to its involvement in this pathway, phosphopentose epimerase is an important enzyme for the cellular response to oxidative stress.
Evolution
The structures of many phosphopentose epimerase analogs have been discovered through crystallographic studies.[13][14] Due to its role in the Calvin cycle and the pentose phosphate pathway, the overall structure is conserved. When the sequences of evolutionarily-distant organisms were compared, greater than 50% similarity was observed.[15] However, amino acids positioned at the dimer interface – which are involved in many intermolecular interactions – are not necessarily conserved. It is important to note that the members of the “ribulose phosphate binding” superfamily resulted from divergent evolution from a (β/α)8 - barrel ancestor.[1]
Drug targeting and malaria
The
See also
- Phosphopentose Isomerase
- Phosphoribulose Kinase
- Pentose Phosphate Pathway
- TIM barrel
- RPE (human gene encoding Ribulose-phosphate 3-epimerase)
References
- ^ PMID 16489742.
- ^ PMID 20923965.
- .
- PMID 1429456.
- PMID 9733539.
- PMID 6882362.
- ^ "Ribulose-phosphate 3-epimerase". UniProt. Retrieved 6 March 2013.
- ^ PMID 12547196.
- ^ Das, Debajoyti (1978). Biochemistry. Academic Publishers. pp. 454–460.
- PMID 4560420.
- ^ ISBN 978-0-7167-8724-2.
- PMID 9890975.
- S2CID 4215318.
- PMID 15333955.
- S2CID 34359563.
- ^ S2CID 9256275.