The enzyme, found in the intestinal mucosa, hydrolyses beta-D-glucosyl and beta-D-galactosyl residues from a very broad range of substrates using a retaining mechanism. Characterized substrates include glucosyl- and galactosyl-ceramides , O3-, O4'- and O7-glucosylated flavonoids , and the 2'-O-glucosylated dihydrochalcone phlorizin . The enzyme includes two glycosyl hydrolase domains, both belonging to the GH1 family. While one domain is responsible for the activity described here, the other catalyses the reaction of EC 3.2.1.108, lactase [4,5]. cf. EC 3.2.1.45, glucosylceramidase and EC 3.2.1.46, galactosylceramidase.
lactase-phlorizin hydrolase, phlorizin hydrolase, cerebrosidase, endoglycoceramidase ii, glycosylceramidase, egcrp1, egcii, endoglycoceramidase-related protein 1, phloretin-glucosidase, endo-glycoceramidase ii, more
The enzyme, found in the intestinal mucosa, hydrolyses beta-D-glucosyl and beta-D-galactosyl residues from a very broad range of substrates using a retaining mechanism. Characterized substrates include glucosyl- and galactosyl-ceramides [3], O3-, O4'- and O7-glucosylated flavonoids [6], and the 2'-O-glucosylated dihydrochalcone phlorizin [1]. The enzyme includes two glycosyl hydrolase domains, both belonging to the GH1 family. While one domain is responsible for the activity described here, the other catalyses the reaction of EC 3.2.1.108, lactase [4,5]. cf. EC 3.2.1.45, glucosylceramidase and EC 3.2.1.46, galactosylceramidase.
coexpression with Rab4S22N or Rab11S25N decreases the number of vesicular structures positive for LPH. Trafficking delay of LPH following Rab protein depletion in MDCK cells
Genotyping of the lactase-phlorizin hydrolase c/t-13910 polymorphism by means of a new rapid denaturing high-performance liquid chromatography-based assay in healthy subjects and colorectal cancer patients.
Krabbe's globoid cell leucodystrophy. Studies on galactosylceramide beta-galactosidase and non-specific beta-galactosidase of leucocytes, cultured skin fibroblasts, and amniotic fluid cells.
Immunoelectrophoretic studies on human small intestinal brush border proteins. A quantitative study of brush border enzymes from single small intestinal biopsies.
Cross-talks among GBA mutations, glucocerebrosidase, and ?-synuclein in GBA-associated Parkinson's disease and their targeted therapeutic approaches: a comprehensive review.
Biogenesis of intestinal lactase-phlorizin hydrolase in adults with lactose intolerance. Evidence for reduced biosynthesis and slowed-down maturation in enterocytes.
Correlation between lactose absorption and the C/T-13910 and G/A-22018 mutations of the lactase-phlorizin hydrolase (LCT) gene in adult-type hypolactasia.
Genotyping of the lactase-phlorizin hydrolase c/t-13910 polymorphism by means of a new rapid denaturing high-performance liquid chromatography-based assay in healthy subjects and colorectal cancer patients.
The effects of adult-type hypolactasia on body height growth and dietary calcium intake from childhood into young adulthood: a 21-year follow-up study--the Cardiovascular Risk in Young Finns Study.
activity in CHOP cell lysates transformed with cDNA encoding KlrP, with conduritol B epoxide, C6-4-nitrobenzo-2-oxa-1,3-diazole-glucosylceramide as substrate
activity in CHOP cell lysates transformed with cDNA encoding KlrP, without conduritol B epoxide, C6-4-nitrobenzo-2-oxa-1,3-diazole-glucosylceramide as substrate
activity in CHOP cell lysates transformed with cDNA encoding KlrP, with conduritol B epoxide, C6-4-nitrobenzo-2-oxa-1,3-diazole-galactosylceramide as substrate
activity in CHOP cell lysates transformed with cDNA encoding KlrP, without conduritol B epoxide, C6-4-nitrobenzo-2-oxa-1,3-diazole-galactosylceramide as substrate
sequential passage of LPH through Rab4-, Rab8- and Rab11-containing compartments. Trafficking of LPH from the TGN to the cell surface can be modulated by dominant-negative Rab8
The profragment, LPHalpha, comprises homologous domains I and II and functions as an intramolecular chaperone in the context of the brush-border LPHbeta region of LPH
LPH encompasses four homologous domains, which presumably have evolved from two subsequent duplications of one ancestral gene, domain organization, overview. The profragment, LPHalpha, comprises homologous domains I and II and functions as an intramolecular chaperone in the context of the brush-border LPHbeta region of LPH. Inter-relationship between homologous domains III and IV of LPHbeta implication in the overall structure, function, and trafficking of LPH, overview. Isolated homologous domain III is transport-competent per se and sorted to the apical membrane in polarized cells. Nevertheless, it neither dimerizes nor acquires complete phlorizin hydrolase activity
pro-enzyme is cleaved in trans-Golgi network between Arg734 and Leu735, pro-region of enzyme is an intramolecular chaperone, analysis of processing and folding
the mutant protein is malfolded and enzymatically inactive and can not exit the endoplasmic reticulum. The mutation creates an additional N-glycosylation site that is characteristic of a temperature-sensitive protein. The potential glycosylation site generated by the mutation is not the cause of defective trafficking of LPH-G1363S or its reduced enzymatic activity. Intracellular transport and enzymatic activity, but not correct folding are partially restored by expression at 20°C. The mutant is responsible for an increased turnover rate
introduction of potential N-glycosylation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency
introduction of potential N-glycosylation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency
introduction of potential N-glycosylation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency
loop-out mutagenesis and construction of deletion or individual domain forms of LPH. Removal of domain IV, which contains lactase, results in a diminished phlorizin hydrolase activity, lack of dimerization in the endoplasmic reticulum, but accelerated transport kinetics from the endoplasmic reticulum to the Golgi apparatus. By contrast, deletion of domain III, which harbors phlorizin hydrolase, generates a malfolded protein that is blocked in the endoplasmic reticulum. Transport kinetics and enzyme activity of LPH and deletion mutants differ
the naturally occurring polymorphism T13910C, i.e. rs4988235, causes lactose intolerance in the C-variant, associated with lower dietary calcium intake and serum calcium levels but not with BMD or fractures. Genotyping and phenotype, overview. The polymorphism is not associated with the genetic variations in the VDR gene, and no interactions between the two genotypes
removal of domain I (LPHDELTA1) results in a malfolded ER-localized protein. Enzyme without domain II (LPHDELTA2) is normally transported along the secretory pathway, but does not dimerize nor is enzymatically active. The lactase activity is not detectable in LPHDELTA1 and LPHDELTA2. Phlorizin hydrolase activity is only detectable in LPHDELTA2, albeit at substantially reduced levels of 4.3%
expression in Chinese hamster ovary-derived cells expressing polyoma LT antigen, in HEK293 cells cotransfected with in KlrP siRNA, overexpression in Escherichia coli
rotavirus infection impairs LPH activity in intestinal cells, the decrease in enzyme activity is not Ca2+- and cAMP-dependent, the LPH biosynthesis, stability, and expression is not modified, the impairment of lactase enzymatic activity during rotavirus infection results from an inhibitory action of the secreted non-structural rotavirus protein NSP4
Impact of O-glycosylation on the function of human intestinal lactase-phlorizin hydrolase. Characterization of glycoforms varying in enzyme activity and localization of O-glycoside addition
Mantei, N.; Villa, M.; Enzler, T.; Wacker, H.; Boll, W.; James, P.; Hunziker, W.; Semenza, G.
Complete primary structure of human and rabbit lactase-phlorizin hydrolase: implications for biosynthesis, membrane anchoring and evolution of the enzyme
Koek, W.; van Meurs, J.; van der Eerden, B.; Rivadeneira, F.; Zillikens, M.; Hofman, A.; Obermayer-Pietsch, B.; Lips, P.; Pols, H.; Uitterlinden, A.; van Leeuwen, J.
The T-13910C polymorphism in the lactase phlorizin hydrolase gene is associated with differences in serum calcium levels and calcium intake