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Information on EC 5.3.1.29 - ribose 1,5-bisphosphate isomerase and Organism(s) Thermococcus kodakarensis and UniProt Accession Q5JFM9

for references in articles please use BRENDA:EC5.3.1.29
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IUBMB Comments
This archaeal enzyme is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The enzyme is activated by cAMP .
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This record set is specific for:
Thermococcus kodakarensis
UNIPROT: Q5JFM9
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Word Map
The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
r15pi, ph0208, r15p isomerase, ribulose 1,5-bisphosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R15P isomerase
-
-
-
-
ribulose 1,5-bisphosphate synthase
-
-
-
-
RuBP synthase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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].
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 SUBSTRATE
NATURAL 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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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
pH 8.3, 85°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29.2
alpha-D-ribose 1,5-bisphosphate
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
pH 8.3, 85°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29.3
pH 8.0, 85°C, wild-type enzyme
32.3
85°C, pH not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C133A
inactive mutant enzyme
C133S
inactive mutant enzyme
D202N
inactive mutant enzyme
R227R
mutant enzyme exhibits a decrease in molecular size of the enzyme and significantly decreases the enzymatic activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased protein levels of the ribose 1,5-bisphosphate isomerase in the cells cultivated with nucleosides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Aono, R.; Sato, T.; Yano, A.; Yoshida, S.; Nishitani, Y.; Miki, K.; Imanaka, T.; Atomi, H.
Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway
J. Bacteriol.
194
6847-6855
2012
Thermococcus kodakarensis (Q5JFM9), Thermococcus kodakarensis
Manually annotated by BRENDA team
Sato, T.; Atomi, H.; Imanaka, T.
Archaeal type III RuBisCOs function in a pathway for AMP metabolism
Science
315
1003-1006
2007
Thermococcus kodakarensis (Q5JFM9)
Manually annotated by BRENDA team
Nakamura, A.; Fujihashi, M.; Aono, R.; Sato, T.; Nishiba, Y.; Yoshida, S.; Yano, A.; Atomi, H.; Imanaka, T.; Miki, K.
Dynamic, ligand-dependent conformational change triggers reaction of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1
J. Biol. Chem.
287
20784-20796
2012
Thermococcus kodakarensis (Q5JFM9)
Manually annotated by BRENDA team