Structure-function analysis of human sucrase-isomaltase identifies key residues required for catalytic activity (Q46363798)

4 July 2018

title

Structure-function analysis of human sucrase-isomaltase identifies key residues required for catalytic activity (English)

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4 July 2018

Mahdi Amiri

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Birthe Gericke

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4 July 2018

Natalie Schecker

series ordinal

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4 July 2018

Hassan Y Naim

series ordinal

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4 July 2018

language of work or name

English

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publication date

18 May 2017

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4 July 2018

Journal of Biological Chemistry

published in

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4 July 2018

volume

292

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4 July 2018

issue

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4 July 2018

page(s)

11070-11078

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4 July 2018

The clinical consequences of sucrase-isomaltase deficiency

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The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities

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Sucrase is an intramolecular chaperone located at the C-terminal end of the sucrase-isomaltase enzyme complex

10 July 2018

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10 July 2018

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Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme

10 July 2018

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Rotavirus infection reduces sucrase-isomaltase expression in human intestinal epithelial cells by perturbing protein targeting and organization of microvillar cytoskeleton.

10 July 2018

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Plant alpha-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin

10 July 2018

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Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit

10 July 2018

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Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment

10 July 2018

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Congenital sucrase-isomaltase deficiency

10 July 2018

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10 July 2018

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10 July 2018

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10 July 2018

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10 July 2018

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10 July 2018

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Human lysosomal alpha-glucosidase. Characterization of the catalytic site

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Action of intestinal sucrase-isomaltase and its free monomers on an alpha-limit dextrin

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Luminal substrate "brake" on mucosal maltase-glucoamylase activity regulates total rate of starch digestion to glucose

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Quaternary and domain structure of glycoprotein processing glucosidase II

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MULTIPLICITY OF HUMAN INTESTINAL DISACCHARIDASES. I. CHROMATOGRAPHIC SEPARATION OF MALTASES AND OF TWO LACTASES.

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Expression of a full-length cDNA coding for human intestinal lactase-phlorizin hydrolase reveals an uncleaved, enzymatically active, and transport-competent protein

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Impact of high pyruvate concentration on kinetics of rabbit muscle lactate dehydrogenase

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Miglustat-induced intestinal carbohydrate malabsorption is due to the inhibition of α-glucosidases, but not β-galactosidases

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Partial amino acid sequences around the essential carboxylate in the active sites of the intestinal sucrase-isomaltase complex

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Identifiers

DOI

10.1074/JBC.M117.791939

1 reference

4 July 2018

PMC publication ID

5491789

1 reference

4 July 2018

PubMed publication ID

28522605

1 reference

4 July 2018