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Information on EC 5.3.1.6 - ribose-5-phosphate isomerase and Organism(s) Homo sapiens

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IUBMB Comments
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
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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 expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
rpi, ribose-5-phosphate isomerase, phosphoriboisomerase, ribose phosphate isomerase, ctrpi, d-ribose-5-phosphate isomerase, ribosephosphate isomerase b, ribosephosphate isomerase a, ribose-5-phosphate isomerase b, ribose 5-phosphate isomerase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-Phosphoribose isomerase
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-
-
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D-Ribose 5-phosphate isomerase
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-
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D-ribose-5-phosphate ketol-isomerase
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-
-
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D-xylose ketol-isomerase
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-
-
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Isomerase, ribose phosphate
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-
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Phosphopentoisomerase
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-
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Phosphopentose isomerase
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-
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Phosphoriboisomerase
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-
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Ribose phosphate isomerase
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Ribose-5-P isomerase
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-
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Ribosephosphate isomerase A
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-
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Ribosephosphate isomerase B
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-
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RPI
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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-
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isomerization
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SYSTEMATIC NAME
IUBMB Comments
D-ribose-5-phosphate aldose-ketose-isomerase
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-83-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
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-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2
D-ribose 5-phosphate
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
in colon cancer cell lines, RPIA enters the nucleus to form a complex with the adenomatous polyposis coli and beta-catenin
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
knockdown or genomic deletion of RPIA results in an increase of ATG4B proteases-mediated processing of autosome marker protein LC3 and in the appearance of LC3-positive autophagosomes in cells. Increased LC3 processing upon knockdown of RPIA can be reversed by treatment with N-acetyl cysteine
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RPIA_HUMAN
311
0
33269
Swiss-Prot
Mitochondrion (Reliability: 4)
Q53SB2_HUMAN
60
0
6512
TrEMBL
other Location (Reliability: 3)
Q53R32_HUMAN
177
0
19597
TrEMBL
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of structures and active sites of RpiB from Leishmania major and RpiA and docking of substrate. Both enzymes form a homomultimer, which in the enzymes of type B is essential to form the active site. Distinct residue types participate in the catalytic reaction in the two enzymes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
RPIA is significantly elevated in colorectal. RPIA modulates cell proliferation and oncogenicity via activation of beta-catenin in colon cancer cell lines. RPIA enters the nucleus to form a complex with the adenomatous polyposis coli and beta-catenin, the association protects beta-catenin by preventing its phosphorylation, ubiquitination, and subsequent degradation. The C-terminus of RPIA (amino acids 290 to 311) is necessary for RPIA-mediated tumorigenesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noltmann, E.A.
Aldose-ketose isomerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
271-354
1972
Echinococcus granulosus, Homo sapiens, Klebsiella aerogenes, Pediococcus pentosaceus, Rhodospirillum rubrum, Saccharomyces cerevisiae, Spinacia oleracea
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Manually annotated by BRENDA team
Heintze, J.; Costa, J.R.; Weber, M.; Ketteler, R.
Ribose 5-phosphate isomerase inhibits LC3 processing and basal autophagy
Cell. Signal.
28
1380-1388
2016
Homo sapiens (P49247)
Manually annotated by BRENDA team
Capriles, P.V.; Baptista, L.P.; Guedes, I.A.; Guimaraes, A.C.; Custodio, F.L.; Alves-Ferreira, M.; Dardenne, L.E.
Structural modeling and docking studies of ribose 5-phosphate isomerase from Leishmania major and Homo sapiens a comparative analysis for Leishmaniasis treatment
J. Mol. Graph. Model.
55
134-147
2015
Homo sapiens (P49247), Leishmania major (Q4Q869)
Manually annotated by BRENDA team
Chou, Y.; Jiang, J.; Yang, M.; Lu, J.; Lin, H.; Wang, H.; Yuh, C.
Identification of a noncanonical function for ribose-5-phosphate isomerase A promotes colorectal cancer formation by stabilizing and activating beta-catenin via a novel C-terminal domain
PLoS Biol.
16
e2003714
2018
Homo sapiens (P49247), Homo sapiens
Manually annotated by BRENDA team