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

BRENDA support

Literature summary for 2.7.1.1 extracted from

  • Lilie, H.; Baer, D.; Kettner, K.; Weininger, U.; Balbach, J.; Naumann, M.; Mueller, E.C.; Otto, A.; Gast, K.; Golbik, R.; Kriegel, T.
    Yeast hexokinase isoenzyme ScHxk2: stability of a two-domain protein with discontinuous domains (2011), Protein Eng. Des. Sel., 24, 79-87.
    View publication on PubMed

General Stability

General Stability Organism
the stability and folding of yeast hexokinase isoenzyme ScHxk2 consisting of two domains with a discontinuous peptide sequence is analysed. Thermodynamic and spectroscopic analyses of urea-induced structural transitions indicate a thermodynamically stable folding intermediate, which is enzymatically inactive. Both structural domains are partially denatured in this central intermediate, even though tryptophan fluorescence, dynamic light scattering (DLS) and one-dimensional 1H NMR indicate a still compact but non-native structure Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P04807
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-glucose
-
Saccharomyces cerevisiae ADP + D-glucose 6-phosphate
-
?

Subunits

Subunits Comment Organism
monomer
-
Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
ScHXK2
-
Saccharomyces cerevisiae