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Information on EC 5.1.3.1 - ribulose-phosphate 3-epimerase and Organism(s) Homo sapiens

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.1 ribulose-phosphate 3-epimerase
IUBMB Comments
The enzyme also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
rpe, d-ribulose-5-phosphate 3-epimerase, ribulose 5-phosphate 3-epimerase, ribulose-5-phosphate 3-epimerase, ribulose-phosphate 3-epimerase, d-ribulose 5-phosphate 3-epimerase, pentose-5-phosphate 3-epimerase, r5p3e, cyt-rpease, d-ribulose-5-phosphate-3-epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-ribulose 5-phosphate 3-epimerase
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D-Ribulose phosphate-3-epimerase
-
-
-
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D-Ribulose-5-P 3-epimerase
-
-
-
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D-Ribulose-5-phosphate epimerase
-
-
-
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D-Xylulose-5-phosphate 3-epimerase
-
-
-
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Epimerase, ribulose phosphate 3-
-
-
-
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Pentose-5-phosphate 3-epimerase
-
-
-
-
Phosphoketopentose 3-epimerase
-
-
-
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Phosphoketopentose epimerase
-
-
-
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Phosphoribulose epimerase
-
-
-
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PPE
-
-
-
-
R5P3E
-
-
-
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Ribulose 5-phosphate 3-epimerase
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-
-
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Ribulose phosphate 3-epimerase
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-
-
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Xylulose phosphate 3-epimerase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-ribulose-5-phosphate 3-epimerase
The enzyme also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-20-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
RPE uses Fe2+ for catalysis
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RPE_HUMAN
228
0
24928
Swiss-Prot
other Location (Reliability: 2)
RPEL1_HUMAN
228
0
25023
Swiss-Prot
other Location (Reliability: 2)
C9J9T0_HUMAN
191
0
20972
TrEMBL
other Location (Reliability: 2)
C9IZU8_HUMAN
225
0
24916
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
-
2 * 23000, SDS-PAGE
45000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 23000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 25% (w/v) PEG 3350, 100 mM Bis-Tris (pH 5.5), and 200 mM NaCl
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D175A
inactive
D37A
the mutation almost abolishes the enzymatic activity
H35A
the mutation almost abolishes the enzymatic activity
H70A
completely insoluble
L12A
the mutation results in more than 50% decrease in the activity
M141A
the mutation results in about 30% decrease in the activity
M39A
the mutation results in about 10% decrease in the activity
M72A
the mutation results in an almost 50% decrease in the activity
S10A
the mutation almost abolishes the enzymatic activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-affinity column chromatography and Superdex G75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme with half normal activity in a malformed and severely mentally retarded girl with a de novo interstitial deletion 46,XX.del(2)(q32.lq34). It is suggested that the gene for ribulose-phosphate 3-epimerase is located on the segment 2q32.1 to q34
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expressed in Escherichia coli BL21(DE3) cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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direct assay procedure which exploits differences in CD spectrum between ribulose 5-phosphate and xylulose 5-phosphate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Karmali, A.; Drake, A.F.; Spencer, N.
Purification, properties and assay of D-ribulose 5-phosphate 3-epimerase from human erythrocytes
Biochem. J.
211
617-623
1983
Homo sapiens
Manually annotated by BRENDA team
Miyazaki, K.; Yamanaka, T.; Ogasawara, N.
Interstitial deletion 2q32.1-->q34 in a child with half normal activity of ribulose 5-phosphate 3-epimerase (RPE)
J. Med. Genet.
25
850-851
1988
Homo sapiens
Manually annotated by BRENDA team
Dallapiccola, B.; Novelli, G.; Giannotti, A.
Deletion 2q31.3-->2q33.3: gene dosage effect of ribulose 5-phosphate 3-epimerase
Hum. Genet.
79
92
1988
Homo sapiens
Manually annotated by BRENDA team
Liang, W.; Ouyang, S.; Shaw, N.; Joachimiak, A.; Zhang, R.; Liu, Z.J.
Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE
FASEB J.
25
497-504
2011
Homo sapiens (Q96AT9), Homo sapiens
Manually annotated by BRENDA team