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Literature summary for 2.7.1.1 extracted from

  • Nawaz, M.H.; Ferreira, J.C.; Nedyalkova, L.; Zhu, H.; Carrasco-Lopez, C.; Kirmizialtin, S.; Rabeh, W.M.
    The catalytic inactivation of the N-half of human hexokinase 2 and structural and biochemical characterization of its mitochondrial conformation (2018), Biosci. Rep., 38, BSR20171666 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli using Champion pET SUMO expression system Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of HK2 in complex with glucose and glucose-6-phosphate. Crystals of DELTA16-hexokinase 2 are grown by sitting-drop vapor diffusion at 18°C Homo sapiens

Protein Variants

Protein Variants Comment Organism
D209A 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 Homo sapiens
D657A 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 Homo sapiens

General Stability

General Stability Organism
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 Homo sapiens
the interaction of HK2 with the mitochondria through its N-half is proposed to facilitate higher stability on the mitochondria Homo sapiens
the N-domain of HK2 regulates the stability of the whole enzyme in contrast with the C-domain Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol structural and biochemical characterization of the mitochondrial conformation reveals higher conformational stability and slow protein unfolding rate compared with the cytosolic conformation Homo sapiens 5829
-
mitochondrion hexokinase 2 is overexpressed in all aggressive tumors and predominantly found on the outer mitochondrial membrane. Structural and biochemical characterization of the mitochondrial conformation reveals higher conformational stability and slow protein unfolding rate compared with the cytosolic conformation. The interaction of hexokinase 2 with the mitochondria through its N-half is proposed to facilitate higher stability on the mitochondria Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P52789
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
hexokinase 2
-
 Homo sapiens
HK2
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
33
-
 D209A mutant enzyme Homo sapiens
37
-
 wild-type enzyme Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
34
-
 Tm-value, wild-type enzyme Homo sapiens
42
-
 Tm-value, wild-type enzyme, addition of glucose Homo sapiens

General Information

General Information Comment Organism
drug target the identification of structural and biochemical differences between HK2 and other human hexokinase isozymes could potentially be used in the development of new anticancer therapies Homo sapiens
metabolism the high proliferation rate of tumor cells demands high energy and metabolites that are sustained by a high glycolytic flux known as the Warburg effect. The activation and further metabolism of glucose is initiated by hexokinase, a focal point of metabolic regulation Homo sapiens
physiological function hexokinase 2 is overexpressed in all aggressive tumors and predominantly found on the outer mitochondrial membrane, where interactions through its N-terminus initiates and maintains tumorigenesis Homo sapiens