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However, glucokinase is coded by a separate gene and its distinctive kinetic properties allow it to serve a different set of functions. Glucokinase has a lower affinity for glucose than the other hexokinases do, and its activity is localized to a few cell types, leaving the other three hexokinases as more important preparers of glucose for ...
The glucokinase regulatory protein (GKRP) also known as glucokinase (hexokinase 4) regulator (GCKR) is a protein produced in hepatocytes (liver cells). GKRP binds and moves glucokinase (GK), thereby controlling both activity and intracellular location [1] [2] of this key enzyme of glucose metabolism. [3] GKRP is a 68 kD protein of 626 amino acids.
231103 Ensembl ENSG00000084734 ENSMUSG00000059434 UniProt Q14397 Q91X44 RefSeq (mRNA) NM_001486 NM_144909 NM_001374741 RefSeq (protein) NP_001477 NP_659158 NP_001361670 Location (UCSC) Chr 2: 27.5 – 27.52 Mb Chr 5: 31.45 – 31.48 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Glucokinase regulator is a protein that in humans is encoded by the GCKR gene. Function This gene encodes ...
In enzymology, an ADP-specific glucokinase (EC 2.7.1.147) also known as ADP-dependent glucokinase is an enzyme that catalyzes the chemical reaction. ADP + D-glucose AMP + D-glucose 6-phosphate. Thus, the two substrates of this enzyme are ADP and D-glucose, whereas its two products are AMP and D-glucose 6-phosphate.
These loss-of-function mutations result in a glucokinase molecule that is less sensitive or less responsive to rising levels of glucose. The beta cells in MODY 2 have a normal ability to make and secrete insulin, but do so only above an abnormally high threshold (e.g., 126–144 mg/dl, or 7-8 mM).
For about 3 hours after a carbohydrate-containing meal, high insulin levels direct liver cells to take glucose from the blood, to convert it to glucose-6-phosphate (G6P) with the enzyme glucokinase, and to add the G6P molecules to the ends of chains of glycogen (glycogen synthesis).
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