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

BRENDA support

Literature summary for 2.7.1.1 extracted from

  • Larion, M.; Miller, B.G.
    23-Residue C-terminal alpha-helix governs kinetic cooperativity in monomeric human glucokinase (2009), Biochemistry, 48, 6157-6165.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild type and mutant enzymes are expressed as N-terminal hexa-histidine tagged polypeptides in glucokinase-deficient Escherichia coli K-12 strain BM5340(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
D205A mutant shows almost no activity Homo sapiens
additional information removal of helix alpha13 abolishes cooperativity and restores Michaelis-Menten kinetics, while reducing the kcat value of the wild type enzyme by 160fold, the impaired catalytic activity of the truncated enzyme is not rescued by the trans-addition of a synthetic alpha13 peptide Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography and Superose 6 gel filtration Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
monomer
-
Homo sapiens

Synonyms

Synonyms Comment Organism
glucokinase
-
Homo sapiens
hexokinase IV
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00091
-
D-glucose mutant enzyme D205A, kcat less than 0.00091 s-1 Homo sapiens
0.18
-
D-glucose truncated enzyme with removed helix alpha13 Homo sapiens
29
-
D-glucose wild type enzyme Homo sapiens
37
-
D-glucose glucokinase with C-terminal 5 alanine addition Homo sapiens
38
-
D-glucose glucokinase with C-terminal 10 alanine addition Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens