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GeneQ18033564· pop 5· linked from 323 articles

Also known as MG, MGA, Maltase-glucoamylase

Maltase-glucoamylase, intestinal is an enzyme that in humans is encoded by the MGAM gene.

In the Vinony graph

Within Vinony's link graph, MGAM is referenced by 323 other articles, and connects out to PubMed, Ensembl genome database project and Wikidata.

It sits within the topics Genes on human chromosome 7 and Human proteins.

Its subject is documented across 5 Wikipedia language editions.

Gene data

MGAM
Name
maltase-glucoamylase
Type
protein-coding
Position
141,907,813–142,106,747 (+)
Aliases
MG, MGA
RefSeq RNA
NM_001365693.1, NM_004668.3, XM_011516670.3, XM_011516671.3, XM_011516672.3
RefSeq protein
NP_001352622.1, NP_004659.2, XP_011514972.1, XP_011514973.1, XP_011514974.1

This gene encodes maltase-glucoamylase, which is a brush border membrane enzyme that plays a role in the final steps of digestion of starch. The protein has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. [provided by RefSeq, Jul 2008].

via MyGene.info

Gene · Ensembl

maltase-glucoamylase

Symbol
MGAM
Biotype
Protein coding
Organism
Homo sapiens
Location
7:141,907,813-142,106,747
Strand
Forward (+)
Assembly
GRCh38
View on Ensembl →

via Ensembl · EMBL-EBI

Wikidata facts

Instance of
gene
Image
PDB 2qly EBI.png
Show 8 more facts
HomoloGene ID
130099
found in taxon
Homo sapiens
cytogenetic location
7q34
genomic start
141607613
genomic end
141806547
expressed in
renal cortex
Sources (3)

via Wikidata · CC0

~4 min read

Encyclopedic overview

10 sections
Contents
  • Gene
  • Tissue distribution
  • Enzymatic mechanism
  • Structure
  • N-terminal maltase
  • C-terminal glucase
  • See also
  • References
  • Further reading
  • External links

Maltase-glucoamylase, intestinal is an enzyme that in humans is encoded by the MGAM gene.

Maltase-glucoamylase is an alpha-glucosidase digestive enzyme. It consists of two subunits with differing substrate specificity. Recombinant enzyme studies have shown that its N-terminal catalytic domain has highest activity against maltose, while the C-terminal domain has a broader substrate specificity and activity against glucose oligomers. In the small intestine, this enzyme works in synergy with sucrase-isomaltase and alpha-amylase to digest the full range of dietary starches.

Excerpted from Wikipedia’s “MGAM” article, available under the CC BY-SA 4.0 licence.

Available in 5 languages

via Wikidata sitelinks · CC0

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