Lactase/phlorizin hydrolase

Definition:

Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta-glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.

References:

[1]. J Potter, et al. Human lactase and the molecular basis of lactase persistence. Biochem Genet. 1985 Jun;23(5-6):423-39. [Content Brief]

[2]. Mikko Kuokkanen, et al. Mutations in the translated region of the lactase gene (LCT) underlie congenital lactase deficiency. Am J Hum Genet. 2006 Feb;78(2):339-44. [Content Brief]

[3]. L Zecca, et al. Intestinal lactase-phlorizin hydrolase (LPH): the two catalytic sites; the role of the pancreas in pro-LPH maturation. FEBS Lett. 1998 Sep 18;435(2-3):225-8. [Content Brief]

[4]. Kitti Németh, et al. Deglycosylation by small intestinal epithelial cell beta-glucosidases is a critical step in the absorption and metabolism of dietary flavonoid glycosides in humans. Eur J Nutr. 2003 Jan;42(1):29-42. [Content Brief]

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