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Literature summary for 3.2.1.3 extracted from

  • Sim, L.; Quezada-Calvillo, R.; Sterchi, E.E.; Nichols, B.L.; Rose, D.R.
    Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity (2008), J. Mol. Biol., 375, 782-792.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of the N-terminal catalytic subunit in Drosophila melanogaster S2 cells and secretion of the recombinant protein from the cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
apoenzyme and enzyme complexed with acarbose, X-ray diffraction structure determination and anaylsis at 2.0 A and 1.9 A resolution, respectively Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
acarbose bound to the active site primarily through side-chain interactions with its acarvosine unit, almost no interactions with its glycone rings, binding structure, overview Homo sapiens
additional information structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
brush border
-
Homo sapiens 5903
-
membrane bound Homo sapiens 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
starch + H2O Homo sapiens one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion D-glucose + ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens O43451
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein recombinant N-terminal catalytic subunit secreted from transformed S2 cells Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
epithelial cell small-intestinal brush-border epithelial cells Homo sapiens
-
small intestine
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dextrin + 6 H2O a mixture of shorter linear and branched dextrin chains is hydrolyzed at the nonreducing ends into glucose Homo sapiens 7 D-glucose
-
?
additional information structure of the N-terminal catalytic subunit and the active site, and basis of inhibition and substrate specificity, overview, the catalytic subunit shows higher affinity for longer maltose oligosaccharides Homo sapiens ?
-
?
starch + H2O
-
Homo sapiens D-glucose + ?
-
?
starch + H2O one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion Homo sapiens D-glucose + ?
-
?

Subunits

Subunits Comment Organism
More the enzyme contains an N-terminal subunit, NtMGAM, that is proximal to the membrane-bound end and a C-terminal luminal subunit, CtMGAM, determination of the structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity, overview, NtMGAM has five major structural domains: a trefoil type-Pdomain, residues 1-51, an N-terminal beta-sandwich domain, residues 52–269, a catalytic (beta/alpha)8 barrel domain, residues 270-651, with two inserted loops (i.e. insert 1, residues 367-416, and insert 2, residues 447-492, protruding out between beta3 and alpha3 and between beta4 and alpha4, respectively) a proximal C-terminal domain, residues 652-730, and a distal C-terminal domain, residues 731-868, both with beta-sandwich topologies, structure comparison with other glycosyl hydrolase family 31 enzymes, overview Homo sapiens

Synonyms

Synonyms Comment Organism
maltase-glucoamylase
-
Homo sapiens
MGAM
-
Homo sapiens
More the enzyme belongs to the glycosyl hydrolase family 31 Homo sapiens