Glucokinase

GCK
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGCK, FGQTL3, GK, GLK, HHF3, HK4, HKIV, HXKP, LGLK, MODY2, glucokinase
External IDsOMIM: 138079; MGI: 1270854; HomoloGene: 55440; GeneCards: GCK; OMA:GCK - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_033508
NM_000162
NM_033507

NM_010292
NM_001287386

RefSeq (protein)

NP_001274315
NP_034422

Location (UCSC)n/aChr 11: 5.85 – 5.9 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse
Glucokinase
Identifiers
EC no.2.7.1.2
CAS no.9001-36-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Glucokinase (EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver and pancreas of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia.

Glucokinase (GK) is a hexokinase isozyme, related homologously to at least three other hexokinases.[4] All of the hexokinases can mediate phosphorylation of glucose to glucose-6-phosphate (G6P), which is the first step of both glycogen synthesis and glycolysis. 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 glycolysis and glycogen synthesis for most tissues and organs. Because of this reduced affinity, the activity of glucokinase, under usual physiological conditions, varies substantially according to the concentration of glucose.[5]

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000041798Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Kawai S, Mukai T, Mori S, Mikami B, Murata K (April 2005). "Hypothesis: structures, evolution, and ancestor of glucose kinases in the hexokinase family". Journal of Bioscience and Bioengineering. 99 (4): 320–330. doi:10.1263/jbb.99.320. PMID 16233797.
  5. ^ Iynedjian PB (January 2009). "Molecular physiology of mammalian glucokinase". Cellular and Molecular Life Sciences. 66 (1): 27–42. doi:10.1007/s00018-008-8322-9. PMC 2780631. PMID 18726182.