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2.7.1.1: hexokinase

This is an abbreviated version!
For detailed information about hexokinase, go to the full flat file.

Word Map on EC 2.7.1.1

Reaction

ATP
+
D-glucose
=
ADP
 +
D-glucose 6-phosphate

Synonyms

6-phosphate glucose kinase, AtHXK1, ATP-D-hexose 6-phosphotransferase, ATP-D-hexose-6-phosphotransferase, ATP-dependent hexokinase, ATP: D-glucose 6-phosphotransferase, ATP: D-hexose 6-phosphotransferase, ATP:D-glucose 6-phosphotransferase, ATP:D-hexose 6-phosphotransferase, BmHk, brain form hexokinase, CzHXK1, FgHXK1, FgHXK2, GCK, GK, GKbeta, GlcK, glk, GlkB, glucokinase, glucokinase 1, glucokinase B, glucose ATP phosphotransferase, HaHXK1, hexokinase, hexokinase (phosphorylating), hexokinase 1, hexokinase 2, hexokinase 3, hexokinase 6, hexokinase A, hexokinase D, hexokinase Dor, hexokinase I, hexokinase II, hexokinase III, hexokinase IV, hexokinase PI, hexokinase PII, hexokinase type I, hexokinase type II, hexokinase type IV, hexokinase type IV glucokinase, hexokinase, tumor isozyme, hexokinase-1, hexokinase-10, hexokinase-2, hexokinase-4, hexokinase-5, hexokinase-6, hexokinase-7, hexokinase-8, hexokinase-9, hexokinase-II, hexokinase-like 1, hGK, hGK isoform 1, HK, HK II, HK-1, HK-I, HK-R, HK1, HK2, HK4, HKDC1, HKI, HKII, HKIII, HKL1, HPGLK1, HXK, HXK A, HXK II, Hxk1, HXK10, Hxk2, Hxk3, HXK4, HXK5, HXK6, HXK7, HXK8, HXK9, hxkC, hxkD, kinase, hexo- (phosphorylating), KlHxk1, LGK, LGK2, liver glucokinase, liver glucokinase isoform 2, MODY2 glucokinase, More, muscle form hexokinase, NfGlck, NtHXK1, OsHXK, OsHXK1, OsHXK10, OsHXK2, OsHXK3, OsHXK4, OsHXK5, OsHXK6, OsHXK7, OsHXK9, pHXK, plastid hexokinase, PpHXK1, PpHXK10, PpHXK11, PpHXK2, PpHXK3, PpHXK4, PpHXK5, PpHXK6, PpHXK7, PpHXK8, PpHXK9, Rag5p, ROK hexokinase, ScHK2, ScHXK2, SoHXK1, StHK, STK_23540, StoHK, TbHK1, TbHK2, TcHK, TthHK, type II hexokinase, VIT_18s0001g14230, xprF, Zm.5206, Zm.95484

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.1 hexokinase

General Stability

General Stability on EC 2.7.1.1 - hexokinase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP, 4 mM, no protection against thermal inactivation
-
D-glucose and other hexoses, glycerol and SH-reagents stabilize
-
D-glucose or D-fructose, 5 mM, stabilizes
-
D-glucose protects against inactivation at higher temperatures
D-glucose stabilizes the enzyme through a specific, ligand induced intramolecular transition from an open to a closed conformation
-
D-glucose, 0.1 M, stabilizes, purified enzyme is extremely unstable in absence of glucose
-
D-glucose, D-fructose, D-mannose and high concentrations of glycerol, 10-15% v/v, stabilize the purified enzyme
-
D-glucose, glycerol and thiol-reducing agents stabilize
-
glucose binding enhances the stability of the wild-type enzyme and the single mutant D657A of the C-domain, but it does not increase the stability of the D209A mutant of the N-domain
glycerol increases the stability
-
glycerol, 9-15% v/v, stabilizes
hexokinase type II is extremely unstable, hexose or thiol stabilizes
-
monothioglycerol stabilizes, enzyme activity is highly dependent on maintenance of free SH-groups
-
NaCl slightly destabilizes the enzyme at pH 3.5 and 38.9°C, conditions for low or no aggregation of the enzyme
one cycle of freezing and thawing, no loss of activity
phosphate stabilizes the wild-type monomer of hexokinase I relative to the dimer, D-glucose 6-phosphate stabilizes the dimer relative to the monomer
stability depends on the presence of 1 mM D-glucose, 3 mM mercaptoethanol, and 9% v/v glycerol
-
storage of purified enzyme in D-glucose-containing phosphate buffer enhances its stability
-
sulfhydryl protecting agents stabilize
-
sulfhydryl protecting agents, e.g. DTT or 2-mercaptoethanol, required for optimum stability
the interaction of HK2 with the mitochondria through its N-half is proposed to facilitate higher stability on the mitochondria
the N-domain of HK2 regulates the stability of the whole enzyme in contrast with the C-domain
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