Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.1.26 extracted from

  • Kim, H.; Uhm, T.; Kim, S.; Kim, P.
    Escherichia coli arabinose isomerase and Staphylococcus aureus tagatose-6-phosphate isomerase: Which is a better template for directed evolution of non-natural substrate isomerization? (2010), J. Microbiol. Biotechnol., 20, 1018-1021.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D158G mutation enhances the activity of the enzyme by more than 20% Staphylococcus aureus
F160S mutation enhances the activity of the enzyme by more than 20% Staphylococcus aureus
G132D mutation enhances the activity of the enzyme by more than 20% Staphylococcus aureus
V54A mutation enhances the activity of the enzyme by more than 20% Staphylococcus aureus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information a non-metallic isomerase Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Galactose 6-phosphate
-
Staphylococcus aureus D-Tagatose 6-phosphate
-
?

Synonyms

Synonyms Comment Organism
tagatose-6-phosphate isomerase
-
Staphylococcus aureus