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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.
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).
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 ...
Glycogenolysis takes place in the cells of the muscle and liver tissues in response to hormonal and neural signals. In particular, glycogenolysis plays an important role in the fight-or-flight response and the regulation of glucose levels in the blood.
Glucose is converted into glucose 6-phosphate by the action of glucokinase or hexokinase with conversion of ATP to ADP.; Glucose-6-phosphate is converted into glucose-1-phosphate by the action of phosphoglucomutase, passing through the obligatory intermediate glucose-1,6-bisphosphate.
In a) the allosteric enzyme functions normally. In b), it is inhibited. This type of enzymes presents two binding sites: the substrate of the enzyme and the effectors. Effectors are small molecules which modulate the enzyme activity; they function through reversible, non-covalent binding of a regulatory metabolite in the allosteric site (which ...