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Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase and Organism(s) Rattus norvegicus

for references in articles please use BRENDA:EC3.2.1.3
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IUBMB Comments
Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 alpha-glucosidase, from mammalian intestine, can catalyse similar reactions.
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Rattus norvegicus
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
glucoamylase, amyloglucosidase, acid maltase, maltase-glucoamylase, lysosomal alpha-glucosidase, maltase glucoamylase, gamma-amylase, glucose amylase, gam-1, glucoamylase p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-alpha-D-glucan glucohydrolase
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acid maltase
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alpha-1,4-glucan glucohydrolase
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amyloglucosidase
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exo-1,4-alpha-glucosidase
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GAI
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GAII
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gamma-amylase
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Glucan 1,4-alpha-glucosidase
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glucoamylase
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glucose amylase
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lysosomal alpha-glucosidase
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Meiotic expression upregulated protein 17
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan glucohydrolase
Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 alpha-glucosidase, from mammalian intestine, can catalyse similar reactions.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-08-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
D3ZTX4_RAT
4481
0
512474
TrEMBL
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mRNA and protein levels and the activities of maltase-glucoamylase are reduced in rats fed an indigestible starch diet compared with those fed a regular starch diet. Decreases in di- and tri-methylation of histone H3 at K4, as well as reduced acetylation of histones H3 and H4 on the maltase-glucoamylase gene are associated with a reduction of maltase-glucoamylase gene expression. The reductions of jejunal maltase-glucoamylase levels and activities caused by the indigestible starch diet are regulated at the mRNA level through a decrease in methylation of histone H3 at K4 and reduced acetylation of histones H3 and H4 on the maltase-glucoamylase gene
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimada, M.; Mochizuki, K.; Goda, T.
Methylation of histone H3 at lysine 4 and expression of the maltase-glucoamylase gene are reduced by dietary resistant starch
J. Nutr. Biochem.
24
606-612
2013
Rattus norvegicus (D3ZTX4)
Manually annotated by BRENDA team