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Literature summary for 5.3.1.29 extracted from

  • Gogoi, P.; Kanaujia, S.
    A presumed homologue of the regulatory subunits of eIF2B functions as ribose-1,5-bisphosphate isomerase in Pyrococcus horikoshii OT3 (2018), Sci. Rep., 8, 1891 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.1.29

Activating Compound

Activating Compound Comment Organism Structure
AMP elevates the catalytic efficiency of the enzyme. The binding site of AMP in the enzyme is reported Pyrococcus horikoshii OT3
AMP presence of AMP provides structural stability to the protein Pyrococcus horikoshii
GMP elevates the catalytic efficiency of the enzyme to a lower degree than AMP. The binding site of AMP in the enzyme is reported Pyrococcus horikoshii OT3
GMP GMP binds to the AMP binding site and an additional binding site Pyrococcus horikoshii

Cloned(Commentary)

Cloned (Comment) Organism
-
 Pyrococcus horikoshii
expression in Rosetta (DE3) Escherichia coli cells Pyrococcus horikoshii OT3

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are obtained in hanging-drop vapor-diffusion method at 20°C within a period of 2-7 days Pyrococcus horikoshii OT3
wild-type and mutants C135S and D204N, in complex with AMP and with GMP Pyrococcus horikoshii

Protein Variants

Protein Variants Comment Organism
C135S mutation of catalytic residue, inhibits binding of substrate ribose 1,5-bisphosphate. Mutation does not not alter the binding behavior of AMP to the protein Pyrococcus horikoshii
D204N mutation of catalytic residue. Mutation does not not alter the binding behavior of AMP to the protein Pyrococcus horikoshii

General Stability

General Stability Organism
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 Pyrococcus horikoshii OT3

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O57947
-
-
Pyrococcus horikoshii DSM 12428 O57947
-
-
Pyrococcus horikoshii OT3 O57947
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus horikoshii OT3

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-D-ribose 1,5-bisphosphate
-
 Pyrococcus horikoshii OT3 D-ribulose 1,5-bisphosphate
-
 r

Synonyms

Synonyms Comment Organism
PH0208
-
 Pyrococcus horikoshii
PH0208
-
 Pyrococcus horikoshii OT3
R15Pi
-
 Pyrococcus horikoshii OT3