Information on EC 5.3.1.29 - ribose 1,5-bisphosphate isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.1.29
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RECOMMENDED NAME
GeneOntology No.
ribose 1,5-bisphosphate isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-ribose 1,5-bisphosphate = D-ribulose 1,5-bisphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
nucleoside and nucleotide degradation (archaea)
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purine metabolism
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-ribose 1,5-bisphosphate aldose-ketose-isomerase
This archaeal enzyme is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The enzyme is activated by cAMP [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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activity is extremely low with the substrate alpha-D-ribose 1,5-bisphosphate alone but is more than 40fold activated in the presence of AMP
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
elevates the catalytic efficiency of the enzyme. The binding site of AMP in the enzyme is reported
GMP
elevates the catalytic efficiency of the enzyme to a lower degree than AMP. The binding site of AMP in the enzyme is reported
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
alpha-D-ribose 1,5-bisphosphate
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pH 8.3, 85°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29.2
alpha-D-ribose 1,5-bisphosphate
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pH 8.3, 85°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48.7
alpha-D-ribose 1,5-bisphosphate
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pH 8.3, 85°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29.3
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pH 8.0, 85°C, wild-type enzyme
32.3
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85°C, pH not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Q58018
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440);
F6BCS4
Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5);
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3);
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1);
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in silico analysis of conserved residues and molecular modeling of structure. Protein PH0208 comprises the residues required for ribose-1,5-bisphosphate activity and the residues reuired for dimerization
crystals are obtained in hanging-drop vapor-diffusion method at 20°C within a period of 2-7 days
sitting drop vapor diffusion method at 20°C. Crystal structure of unliganded Tk-R15Pi is solved by means of the single-wavelength anomalous dispersion method using SeMet-substituted enzyme and refined at 2.5 A resolution
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the AMP binding site in PH0208 protein clarifies the role of AMP in providing structural stability to the enzyme. The binding of GMP to the AMP binding site in addition to its own binding site indicates that GMP might also execute a similar function, though with less specificity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Rosetta (DE3) Escherichia coli cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased protein levels of the ribose 1,5-bisphosphate isomerase in the cells cultivated with nucleosides
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C133A
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inactive mutant enzyme
C133S
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inactive mutant enzyme
D202N
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inactive mutant enzyme
R227R
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mutant enzyme exhibits a decrease in molecular size of the enzyme and significantly decreases the enzymatic activity
Show AA Sequence (246 entries)
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