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
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
Thermococcus kodakarensis
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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
Thermococcus kodakarensis
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pH 8.3, 85°C
6393
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
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
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
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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 (160 entries)
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