Congenital Lactose Malabsorption

Levin, B.; Abraham, J. M.; Burgess, E. Ann; Wallis, P. G.

doi:10.1136/adc.45.240.173

Cited by 25 publications

(5 citation statements)

References 10 publications

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“…Some reports in the 1960s were suggestive of lactase deficiency from birth, but they did not absolutely exclude prolonged, secondary lactase deficiency which we now know is relatively common. A recent report (Levin et al, 1970) has at last documented, without any real doubt, the diagnosis of congenital lactase deficiency in an infant first investigated at the age of 3 days and then observed for longer than 2 years. These authors iUustrate the difficulties involved in adequate documentation of this rare disorder.…”

Section: Treatmentmentioning

confidence: 99%

Sugar-induced diarrhoea in children.

Gracey¹,

Burke²

1973

Archives of Disease in Childhood

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Section: Treatmentmentioning

confidence: 99%

Sugar-induced diarrhoea in children.

Gracey¹,

Burke²

1973

Archives of Disease in Childhood

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“…Detailed structure information stemming from crystallography is still required to shed light on the interplay between the activities of both catalytic domains. LPH deficiency causes congenital disaccharide intolerance II, a gastrointestinal disorder characterized by severe diarrhea in infants when fed with lactose as abundantly present in milk (64). The GH1 family also includes the enzyme GBA3, a cytosolic -glucosidase expressed in some cell types.…”

Section: Other Proteins Of Family Gh1 Resembling Glycosylceramidasesmentioning

confidence: 99%

Distinguishing the differences in β-glycosylceramidase folds, dynamics, and actions informs therapeutic uses

Bdira

Artola

Overkleeft

et al. 2018

Journal of Lipid Research

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Glycoconjugates play essential roles in diverse biological processes and abnormalities and have been linked to multiple pathologies. The staggering structural diversity of glycoconjugates stems from the almost infinite possible combinations by which multiple monosaccharide building blocks may be linked with each other (1). For instance, 1,056 unique trisaccharides can be formed just from 3 different monosaccharides. Polysaccharides are very stable compounds: their spontaneous hydrolysis takes place at a rate of 10 15 s 1 , corresponding to a half-life of 4.7 million years (2). To allow for the efficient metabolism of glycoconjugates, enzymes have evolved as specialized catalysts. In most organisms, an estimated 1% to 3% of the genes encode carbohydrate-active enzymes (3). Among these are glycoside hydrolases (GHs) that can enhance the rate of hydrolysis of specific carbohydrate glycosidic bonds in glycoconjugates more than 10 17 times (2). These GH enzymes show marked specificity regarding number, position, and configuration of the hydroxyl groups in their substrate sugar. They are widely applied in biotechnology, for example, in biofuel production, paper pulp bleaching, and the food industry (4, 5). Likewise, specific GH inhibitors are extensively used as agrochemicals and therapeutic agents (6-8). Abnormalities in GHs underlie metabolic disorders in humans, for instance, inherited lysosomal storage disorders and lactose intolerance (9, 10). GH enzymes differ in substrate specificity, mode of enzymatic attack Abstract Glycosyl hydrolases (GHs) are carbohydrate-active enzymes that hydrolyze a specific -glycosidic bond in glycoconjugate substrates; -glucosidases degrade glucosylceramide, a ubiquitous glycosphingolipid. GHs are grouped into structurally similar families that themselves can be grouped into clans. GH1, GH5, and GH30 glycosidases belong to clan A hydrolases with a catalytic (/) 8 TIM barrel domain, whereas GH116 belongs to clan O with a catalytic (/) 6 domain. In humans, GH abnormalities underlie metabolic diseases. The lysosomal enzyme glucocerebrosidase (family GH30), deficient in Gaucher disease and implicated in Parkinson disease etiology, and the cytosol-facing membrane-bound glucosylceramidase (family GH116) remove the terminal glucose from the ceramide lipid moiety. Here, we compare enzyme differences in fold, action, dynamics, and catalytic domain stabilization by binding site occupancy. We also explore other glycosidases with reported glycosylceramidase activity, including human cytosolic -glucosidase, intestinal lactase-phlorizin hydrolase, and lysosomal galactosylceramidase. Last, we describe the successful translation of research to practice: recombinant glycosidases and glucosylceramide metabolism modulators are approved drug products (enzyme replacement therapies). Activity-based probes now facilitate the diagnosis of enzyme deficiency and screening for compounds that interact with the catalytic pocket of glycosidases. Future research may deepen the understanding of the function...

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“…The primary forms consist first of the excessively rare syndrome of congenital alactasia. There have been remarkably few of these cases reported [2,3]. Most have in fact been reported from Finland [4].…”

Section: Lactose Intolerancementioning

confidence: 99%

Milk intolerance in children

Ja¹

1986

Clin Experimental Allergy

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Congenital Lactose Malabsorption

Cited by 25 publications

References 10 publications

Sugar-induced diarrhoea in children.

Sugar-induced diarrhoea in children.

Distinguishing the differences in β-glycosylceramidase folds, dynamics, and actions informs therapeutic uses

Milk intolerance in children

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