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Literature summary for 5.3.1.5 extracted from

  • Rozanov, A.; Zagrebelnyc, S.; Beklemishchev, A.
    Cloning of Escherichia coli K12 xylose isomerase (glucose isomerase) and studying the enzymatic properties of its expression product (2009), Prikl. Biokhim. Mikrobiol., 45, 38-44.
    View publication on PubMed
Search for more literature for 5.3.1.5

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli strain BL21(DE3) from vector pRAC Escherichia coli K-12

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can only partially substitute for Mg2+ Escherichia coli K-12
Mg2+ preferred metal ion, activates by 15-20% Escherichia coli K-12

Organism

Organism UniProt Comment Textmining
Escherichia coli K-12
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by one-step affinity chromatography to over 90% purity Escherichia coli K-12

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Xylose
-
 Escherichia coli K-12 D-Xylulose
-
 ?
additional information the recombinant enzyme catalyzes also the isomerization of D-glucose to D-fructose Escherichia coli K-12 ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 recombinant enzyme Escherichia coli K-12

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 purified recombinant enzyme, rapid inactivation Escherichia coli K-12
65
-
 purified recombinant enzyme, 1 h, complete inactivation Escherichia coli K-12

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 recombinant enzyme Escherichia coli K-12