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IUBMB CommentsAlso acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
rpi, ribose-5-phosphate isomerase, phosphoriboisomerase, ribose phosphate isomerase, ctrpi, d-ribose-5-phosphate isomerase, ribosephosphate isomerase b, ribosephosphate isomerase a, ribose-5-phosphate isomerase b, ribose 5-phosphate isomerase a,
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5-Phosphoribose isomerase
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D-Ribose 5-phosphate isomerase
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D-ribose-5-phosphate ketol-isomerase
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D-xylose ketol-isomerase
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Isomerase, ribose phosphate
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Phosphopentoisomerase
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Phosphopentose isomerase
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Phosphoriboisomerase
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Ribose phosphate isomerase
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Ribose-5-P isomerase
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Ribosephosphate isomerase A
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Ribosephosphate isomerase B
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intramolecular oxidoreduction
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D-ribose-5-phosphate aldose-ketose-isomerase
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
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D-ribose 5-phosphate
D-ribulose 5-phosphate
D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
direct or indirect catalytic role for the residues E107, D85 and K98
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r
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
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0.17 - 7.13
D-ribose 5-phosphate
additional information
additional information
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0.17
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme D85N
1.17
D-ribose 5-phosphate
50°C, pH 6.0, wild-type enzyme
2.39
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme D168N
5.1
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme K125A
7.13
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme R100A
additional information
additional information
dramatic increase of Km-value at temperatures above 80°C
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additional information
additional information
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dramatic increase of Km-value at temperatures above 80°C
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8.3 - 625
D-ribose 5-phosphate
50
D-ribulose 5-phosphate
50°C, pH 6.0, wild-type enzyme
8.3
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme D85N
151
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme K125A
177
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme R100A
312
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme D168N
320
D-ribose 5-phosphate
50°C, pH 6.0, wild-type enzyme
625
D-ribose 5-phosphate
93°C, pH 6, wild-type enzyme
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Uniprot
brenda
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25163
4 * 25163, calculation from nucleotide sequence
26000
4 * 26000, in crystal and in solution, each monomer has a new fold consisting of two alpha/beta domains, SDS-PAGE
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tetramer
4 * 25163, calculation from nucleotide sequence
tetramer
4 * 26000, in crystal and in solution, each monomer has a new fold consisting of two alpha/beta domains, SDS-PAGE
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hanging drop vapor diffusion method, crystal structure of the free enzyme and the complex with D-4-phosphoerythronic acid
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100
stability and integrity up to, needs at least 250 mM NaCl to maintain its hyperthermostability
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overexpression in Escherichia coli
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Ishikawa, K.; Matsui, I.; Payan, F.; Cambillau, C.; Ishida, H.; Kawarabayasi, Y.; Kikuchi, H.; Roussel, A.
A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure
Structure
10
877-886
2002
Pyrococcus horikoshii (O50083), Pyrococcus horikoshii
brenda
5.3.1.6 ribose-5-phosphate isomerase
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