BRENDA - Enzyme Database show
show all sequences of 5.3.1.29

A presumed homologue of the regulatory subunits of eIF2B functions as ribose-1,5-bisphosphate isomerase in Pyrococcus horikoshii OT3

Gogoi, P.; Kanaujia, S.; Sci. Rep. 8, 1891 (2018)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
AMP
presence of AMP provides structural stability to the protein
Pyrococcus horikoshii
AMP
elevates the catalytic efficiency of the enzyme. 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
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
Cloned(Commentary)
Commentary
Organism
-
Pyrococcus horikoshii
expression in Rosetta (DE3) Escherichia coli cells
Pyrococcus horikoshii OT3
Crystallization (Commentary)
Crystallization
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
Engineering
Amino acid exchange
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus horikoshii
O57947
-
-
Pyrococcus horikoshii DSM 12428
O57947
-
-
Pyrococcus horikoshii OT3
O57947
-
-
Purification (Commentary)
Commentary
Organism
-
Pyrococcus horikoshii OT3
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-D-ribose 1,5-bisphosphate
-
746485
Pyrococcus horikoshii OT3
D-ribulose 1,5-bisphosphate
-
-
-
r
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
AMP
presence of AMP provides structural stability to the protein
Pyrococcus horikoshii
AMP
elevates the catalytic efficiency of the enzyme. 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
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
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Pyrococcus horikoshii
expression in Rosetta (DE3) Escherichia coli cells
Pyrococcus horikoshii OT3
Crystallization (Commentary) (protein specific)
Crystallization
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
Engineering (protein specific)
Amino acid exchange
Commentary
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 (protein specific)
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
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pyrococcus horikoshii OT3
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-D-ribose 1,5-bisphosphate
-
746485
Pyrococcus horikoshii OT3
D-ribulose 1,5-bisphosphate
-
-
-
r
Other publictions for EC 5.3.1.29
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746485
Gogoi
A presumed homologue of the r ...
Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428, Pyrococcus horikoshii OT3
Sci. Rep.
8
1891
2018
4
-
2
2
2
1
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7
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1
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1
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4
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2
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2
2
1
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1
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1
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733939
Gogoi
In silico analysis suggests th ...
Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428
Gene
575
118-126
2016
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1
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7
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1
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725279
Aono
Enzymatic characterization of ...
Thermococcus kodakarensis
J. Bacteriol.
194
6847-6855
2012
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-
-
-
-
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1
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1
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3
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1
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1
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1
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2
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1
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1
1
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1
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1
1
1
727903
Nakamura
Dynamic, ligand-dependent conf ...
Thermococcus kodakarensis
J. Biol. Chem.
287
20784-20796
2012
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1
1
4
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3
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1
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1
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1
1
1
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1
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1
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1
4
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1
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1
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1
1
1
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1
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726487
Sato
Archaeal type III RuBisCOs fun ...
Thermococcus kodakarensis
Science
315
1003-1006
2007
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1
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1
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