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Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase and Organism(s) Amorphotheca resinae and UniProt Accession Q03045

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EC Tree
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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Amorphotheca resinae
UNIPROT: Q03045
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Word Map
The taxonomic range for the selected organisms is: Amorphotheca resinae
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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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
show the reaction diagram
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acarbose
binding structure, overview. Found in the active sites of both independent monomers. In both monomers an acarbose molecule is fitted and refined, assuming full occupancy
acarviosine
the inhibitor occupies the active-site pocket with the cyclohexitol moiety of acarviosine populating the -1 subsite
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Hormoconis resinae
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is a member of the glycoside hydrolase family 15 (GH15)
additional information
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMYG_AMORE
616
0
66432
Swiss-Prot
Secretory Pathway (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The full-length structure of HrGA shows extensive N-glycosylation, where the resolved sites are at Asn99, Asn200, Asn427, Asn500, Asn514, Asn528 and Asn587. Asn200 is the only site that shows branching of the glycosylation chain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 150 nl of 37 mg/ml protein in 20 mM sodium acetate, pH 5.0, with 150 nl of reservoir solution containing 60% Tacsimate, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 3.6 A resolution, molecular replacement using the catalytic domain of Aspergillus awamori glucoamylase as a search model (PDB entry 1glm)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Aspergillus niger strain MBin118 by alpha-cyclodextrin affinity chromatography, elution with beta-cyclodextrin, followed by dialysis, to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GAMP, recombinant expression of the enzyme in Aspergillus niger strain MBin118
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Manjunath, P.; Shenoy, B.C.; Raghavendra Roa, M.R.
Fungal glucoamylases
J. Appl. Biochem.
5
235-260
1983
Aspergillus awamori, Aspergillus candidus, Aspergillus foetidus, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Acremonium charticola, Amorphotheca resinae, Coniophora cerebella, Endomyces sp., Thermomyces lanuginosus, Pyricularia grisea, Mucor rouxianus, Rhizopus arrhizus
Manually annotated by BRENDA team
Roth, C.; Moroz, O.V.; Ariza, A.; Skov, L.K.; Ayabe, K.; Davies, G.J.; Wilson, K.S.
Structural insight into industrially relevant glucoamylases flexible positions of starch-binding domains
Acta Crystallogr. Sect. D
74
463-470
2018
Aspergillus niger (P69328), Amorphotheca resinae (Q03045), Penicillium oxalicum (S7ZIW0), Penicillium oxalicum 114-2 (S7ZIW0), Penicillium oxalicum CGMCC 5302 (S7ZIW0)
Manually annotated by BRENDA team