Glycerol kinases

Glycerol kinases
Mass / length primary structure	529-559 amino acids
Identifier
Gene name (s)	GK , GK2 , GK5 , GK3P
Enzyme classification
EC, category	2.7.1.30 , kinase
Response type	Phosphorylation
Substrate	ATP + glycerin
Products	ADP + L-glycerol-3-phosphate
Occurrence
Parent taxon	Creature

The glycerine kinases (GK) are several enzymes that phosphorylate glycerine to glycerine-3-phosphate and thus activate either the breakdown of glycerine or the biosynthesis of the triglycerides . The vertebrate glycerol kinases are homologous to one another . In people four are paralogous enzymes known, and there are from each other isoforms caused by alternative splicing of the mRNA produced, not all molecules enzyme activity possess. GK are localized both on the outside of the mitochondrial membrane and in the cytosol . In humans GK are in liver , kidney and testis expressed . Mutations are only at GK - gene known; the resulting enzyme deficiency is associated with (rare hereditary) hyperglycerinemia .

GKs are also found in the intestinal mucosa and the lactating breast.

Overexpression of GK in rats led to changes in the total carbon metabolism; so there seem to be other functions for the enzyme.

Catalyzed reaction

+ ATP ⇒ + ADP

Glycerine is converted to L-glycerine-3-phosphate.

↑ UniProt P32189
↑ Sriram G, Rahib L, He JS, et al : Global metabolic effects of glycerol kinase overexpression in rat hepatoma cells . In: Mol. Genet. Metab. . 93, No. 2, February 2008, pp. 145-59. doi : 10.1016 / j.ymgme.2007.09.008 . PMID 18029214 .
↑ Rahib L, MacLennan NK, Horvath S, Liao JC, Dipple KM: Glycerol kinase deficiency alters expression of genes involved in lipid metabolism, carbohydrate metabolism, and insulin signaling . In: Eur. J. Hum. Genet. . 15, No. 6, June 2007, pp. 646-57. doi : 10.1038 / sj.ejhg.5201801 . PMID 17406644 .

Wikibooks: Biochemie_und_Pathobiochemie: Triacylglycerolbiosynthesis - learning and teaching materials