Literature summary for 5.3.1.6 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.

Search for more literature for 5.3.1.6

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli	Pyrococcus horikoshii

Crystallization (Commentary)

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

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O50083	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pyrococcus horikoshii

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
tetramer	4 * 25163, calculation from nucleotide sequence	Pyrococcus horikoshii
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]

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

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Release 2023.1 (January 2023)