Sandbox GGC2
From Proteopedia
Glucokinase
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Glucokinase is also known as human hexokinase IV [1]. It is an enzyme that involves in the regulation of glucose homeostasis. Liver and pancreatic cells use glucokinase converts glucose molecule to glucose 6 phosphate. Structure and FunctionGlucokinase is a protein contains 465 amino acid residues which make up two domains, including a small domain and a large domain. When glucose molecule binds to the active site of glucoskinase, it forms hydrogen bonds with Asn 204, Asp 205, Asn 231, Glu 256 and Glu 290. At the allosteric site, either glucokinase activators (GKA) or glucokinase inhibitor (GKI) will bind to regulate the activity of glucokinase by changing the confirmation. JSmol structure shows an example of GK-GKA complex, where the GKA bind to the allosteric site. the allosteric site is composed of 3 hydrophobic pockets which are made up of different amino acid residues colored in pink, green, and dark blue. Among the residues at the allosteric site, only Arg63, Tyr215, and Gln98 involve in hydrogen bond interaction with the GKA.
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This page was last modified 23:52, 28 April 2017.