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Literature summary extracted from

  • 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 (2002), Structure, 10, 877-886.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.6 overexpression in Escherichia coli Pyrococcus horikoshii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.6 hanging drop vapor diffusion method, crystal structure of the free enzyme and the complex with D-4-phosphoerythronic acid Pyrococcus horikoshii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.6 additional information
-
additional information dramatic increase of Km-value at temperatures above 80°C Pyrococcus horikoshii
5.3.1.6 0.17
-
D-ribose 5-phosphate 50°C, pH 6.0, mutant enzyme D85N Pyrococcus horikoshii
5.3.1.6 1.17
-
D-ribose 5-phosphate 50°C, pH 6.0, wild-type enzyme Pyrococcus horikoshii
5.3.1.6 2.39
-
D-ribose 5-phosphate 50°C, pH 6.0, mutant enzyme D168N Pyrococcus horikoshii
5.3.1.6 5.1
-
D-ribose 5-phosphate 50°C, pH 6.0, mutant enzyme K125A Pyrococcus horikoshii
5.3.1.6 7.13
-
D-ribose 5-phosphate 50°C, pH 6.0, mutant enzyme R100A Pyrococcus horikoshii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.6 25163
-
4 * 25163, calculation from nucleotide sequence Pyrococcus horikoshii
5.3.1.6 26000
-
4 * 26000, in crystal and in solution, each monomer has a new fold consisting of two alpha/beta domains, SDS-PAGE Pyrococcus horikoshii
5.3.1.6 98000
-
gel filtration Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.1.6 D-ribose 5-phosphate Pyrococcus horikoshii
-
D-ribulose 5-phosphate
-
r

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.6 Pyrococcus horikoshii O50083
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.6
-
Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.6 D-ribose 5-phosphate
-
Pyrococcus horikoshii D-ribulose 5-phosphate
-
r
5.3.1.6 D-ribose 5-phosphate direct or indirect catalytic role for the residues E107, D85 and K98 Pyrococcus horikoshii D-ribulose 5-phosphate
-
r

Subunits

EC Number Subunits Comment Organism
5.3.1.6 tetramer 4 * 25163, calculation from nucleotide sequence Pyrococcus horikoshii
5.3.1.6 tetramer 4 * 26000, in crystal and in solution, each monomer has a new fold consisting of two alpha/beta domains, SDS-PAGE Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.3.1.6 95
-
-
Pyrococcus horikoshii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.1.6 100
-
stability and integrity up to, needs at least 250 mM NaCl to maintain its hyperthermostability Pyrococcus horikoshii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.6 8.3
-
D-ribose 5-phosphate 50°C, pH 6.0, mutant enzyme D85N Pyrococcus horikoshii
5.3.1.6 50
-
D-ribulose 5-phosphate 50°C, pH 6.0, wild-type enzyme Pyrococcus horikoshii
5.3.1.6 151
-
D-ribose 5-phosphate 50°C, pH 6.0, mutant enzyme K125A Pyrococcus horikoshii
5.3.1.6 177
-
D-ribose 5-phosphate 50°C, pH 6.0, mutant enzyme R100A Pyrococcus horikoshii
5.3.1.6 312
-
D-ribose 5-phosphate 50°C, pH 6.0, mutant enzyme D168N Pyrococcus horikoshii
5.3.1.6 320
-
D-ribose 5-phosphate 50°C, pH 6.0, wild-type enzyme Pyrococcus horikoshii
5.3.1.6 625
-
D-ribose 5-phosphate 93°C, pH 6, wild-type enzyme Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.1.6 6
-
at 50°C Pyrococcus horikoshii