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Glucokinase changes conformation and/or function in parallel with rising glucose concentrations in the physiologically important range of 4–10 M (72–180 mg/dL). It is half-saturated at a glucose concentration of about 8 mM (144 mg/dL). [10] [11] Glucokinase is not inhibited by physiological concentrations of its product, glucose-6-phosphate ...
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).
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.
The gene product is a regulatory protein that inhibits glucokinase in liver and pancreatic islet cells by binding non-covalently to form an inactive complex with the enzyme. This gene is considered a susceptibility gene candidate for a form of maturity onset diabetes of the young (MODY). [provided by RefSeq, Jul 2008].
In enzymology, a gluconokinase (EC 2.7.1.12) is an enzyme that catalyzes the chemical reaction ATP + D-gluconate ⇌ {\displaystyle \rightleftharpoons } ADP + 6-phospho-D-gluconate Thus, the two substrates of this enzyme are ATP and D-gluconate , whereas its two products are ADP and 6-phospho-D-gluconate .
Glycogen debranching enzyme then transfers three of the remaining four glucose units to the end of another glycogen branch. This exposes the α[1→6] branching point, which is hydrolysed by α[1→6] glucosidase , removing the final glucose residue of the branch as a molecule of glucose and eliminating the branch.
The enzymes from yeast, plants and vertebrates all show clear sequence evidence of homology, but those of bacteria may not be related. [ 4 ] They are categorized as actin fold proteins, sharing a common ATP binding site core that is surrounded by more variable sequences which determine substrate affinities and other properties.