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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Aspergillus niger and UniProt Accession P56526
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3.2.1.20 alpha-glucosidaseIUBMB Comments
This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of (1->4)-alpha-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase and, more slowly, hydrolyses (1->6)-alpha-D-glucose links.
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Word Map
- 3.2.1.20
- lactase
- acarbose
- maltose
- lysosomal
- disaccharidase
-
postprandial
- mellitus
- border
-
brush
- pompe
- glycogen
- starch
- alpha-amylase
- mucosal
- aminopeptidase
- hyperglycemia
-
antidiabetic
- jejunal
- amylase
- beta-glucosidase
- sulfonylurea
- meal
- trehalase
- ileum
- glucoamylase
-
glycemic
- metformin
- villus
- glycosidases
- thiazolidinediones
- alpha-mannosidase
-
hypoglycemic
- biguanides
-
brush-border
- glycogenosis
-
sulphonylureas
- alpha-galactosidase
- maltotriose
-
non-insulin-dependent
-
peptidase-4
- 1-deoxynojirimycin
- n-acetyl-beta-glucosaminidase
-
carbohydrases
-
antihyperglycemic
- castanospermine
-
infantile-onset
- alpha-fucosidase
- cellobiase
- medicine
- repaglinide
-
flatulence
- synthesis
- agriculture
- biotechnology
- nutrition
- diagnostics
The taxonomic range for the selected organisms is: Aspergillus niger
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-glucosidase, maltase, neutral alpha-glucosidase, alpha-d-glucosidase, alglucosidase alfa, intestinal maltase, intestinal alpha-glucosidase, alpha-1,4-glucosidase, recombinant human gaa, alpha-glucosidase ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid maltase
-
-
-
-
AGL
alpha-1,4-glucosidase
-
-
-
-
alpha-D-glucosidase
-
-
-
-
alpha-glucopyranosidase
-
-
-
-
alpha-glucosidase
alpha-glucoside hydrolase
-
-
-
-
glucoinvertase
-
-
-
-
glucosidoinvertase
-
-
-
-
glucosidosucrase
-
-
-
-
maltase
-
-
-
-
maltase-glucoamylase
-
-
-
-
additional information
-
the enzyme belongs to the alpha-glucosidase family 31
AGL
-
-
-
-
alpha-glucosidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucoside glucohydrolase
This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of (1->4)-alpha-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase and, more slowly, hydrolyses (1->6)-alpha-D-glucose links.
CAS REGISTRY NUMBER
COMMENTARY
9001-42-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl 2-deoxy-alpha-D-glucopyranoside + H2O
4-nitrophenol + 2-deoxy-alpha-D-glucose
low activity, wild-type and recombinant enzyme
-
-
?
4-nitrophenyl 3-deoxy-alpha-D-glucopyranoside + H2O
4-nitrophenol + 3-deoxy-alpha-D-glucose
very low activity, wild-type and recombinant enzyme
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
very low activity, wild-type and recombinant enzyme
-
-
?
isomaltose
isomaltotriose + alpha-D-glucose
-
-
transglucosylation products
?
panose
alpha-D-glucose + tetrasaccharides
-
-
transglucosylation products
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
preferred substrate of wild-type and recombinant enzyme
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
assay at pH 5.5, 50°C, reaction terminated by sodium carbonate solution
-
-
?
additional information
?
-
no activity of wild-type and recombinant enzyme with 4-nitrophenyl 4-deoxy-alpha-D-glucopyranoside and 4-nitrophenyl 6-deoxy-alpha-D-glucopyranoside
-
-
?
additional information
?
-
synthesis of panose or isomaltose by transglycosylation as a function of the glucosyl acceptor, panose is the main transglycosylation product after 8 h of incubation, whereas isomaltose is predominant after 24 h. Isomaltose also becomes predominant at shorter times if a mixture of maltose and glucose is used instead of maltose
-
-
?
additional information
?
-
-
substrate aglycon specificity profiling, overview
-
-
?
additional information
?
-
immobilized recombinant alpha-glucosidase catalyzes maltose into isomaltooligosaccharides (IMOs) by its transglucosylation activity. The synthesis of IMOs is conducted using maltose as the substrate
-
-
?
additional information
?
-
the recombinant enzyme performs isomaltooligosaccharides (IMOs) synthesis by transglycosylation. Quantitative analyses of products maltose (M), isomaltose (IG2), panose (P), and isomaltotriose (IG3)
-
-
?
additional information
?
-
transglucosylation activity by wild-type and Asn694 mutant enzymes forming isomaltooligosaccharides, overview. Isomaltose and panose are the predominant final products of wild-type alpha-glucosidase
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-anhydro-1-deoxy-1-[(1-oxopentyl-5-hydroxy)amino]-D-glycero-D-ido-heptitol
-
-
2,6-anhydro-7-deoxy-7-([1-(hydroxymethyl)ethenyl]amino)-D-glycero-L-gulo-heptitol
-
-
2,6-anhydro-7-deoxy-7-[(1-methylethenyl)amino]-D-glycero-L-gulo-heptitol
-
-
2,6-anhydro-7-deoxy-7-[(1-phenylethenyl)amino]-D-glycero-L-gulo-heptitol
-
-
2,6-anhydro-7-deoxy-7-[(2,2-dimethyl-1-methylidenepropyl)amino]-D-glycero-L-gulo-heptitol
-
-
2,6-anhydro-7-deoxy-7-[(3-hydroxy-1-methylidenepropyl)amino]-D-glycero-L-gulo-heptitol
-
-
2,6-anhydro-7-deoxy-7-[(4-hydroxy-1-methylidenebutyl)amino]-D-glycero-L-gulo-heptitol
-
-
additional information
-
no inhibition by 2,6-anhydro-7-deoxy-7-[(6-hydroxy-1-methylidenehexyl)amino]-D-glycero-L-gulo-heptitol, IC50 values, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.54
4-Nitrophenyl 2-deoxy-alpha-D-glucopyranoside
pH 4.5, 37°C, wild-type enzyme
6.61
4-Nitrophenyl 2-deoxy-alpha-D-glucopyranoside
pH 4.5, 37°C, recombinant enzyme
10.5
4-nitrophenyl 3-deoxy-alpha-D-glucopyranoside
pH 4.5, 37°C, wild-type enzyme
11.6
4-nitrophenyl 3-deoxy-alpha-D-glucopyranoside
pH 4.5, 37°C, recombinant enzyme
0.59
4-nitrophenyl alpha-D-glucopyranoside
pH 4.5, 37°C, recombinant enzyme
0.62
4-nitrophenyl alpha-D-glucopyranoside
pH 4.5, 37°C, wild-type enzyme
additional information
additional information
kinetics for transglucosylation of wild-type and mutant enzymes, overview
-
additional information
additional information
kinetics of transglucosylation activity of immobilized alpha-glucosidase
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.13
purified recombinant enzyme, substrate 4-nitrophenyl 3-deoxy-alpha-D-glucopyranoside, recombinant enzyme
0.14
purified wild-type enzyme, substrate 4-nitrophenyl 3-deoxy-alpha-D-glucopyranoside, recombinant enzyme
0.96
purified recombinant enzyme, substrate 4-nitrophenyl alpha-D-glucopyranoside, recombinant enzyme
1.06
purified wild-type enzyme, substrate 4-nitrophenyl alpha-D-glucopyranoside, recombinant enzyme
3.7
purified recombinant enzyme, substrate 4-nitrophenyl 2-deoxy-alpha-D-glucopyranoside, recombinant enzyme
4.25
purified wild-type enzyme, substrate 4-nitrophenyl 2-deoxy-alpha-D-glucopyranoside, recombinant enzyme
46.8
purified recombinant enzyme, substrate maltose, recombinant enzyme
57.8
purified wild-type enzyme, substrate maltose, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
3 - 7
-
pH 3.0: about 30% of maximal activity, pH 7.0: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 50
-
5°C: about 50% of maximal activity, 50°C: about 20% of maximal activity, maltase
5 - 80
-
5°C: about 50% of maximal activity, 80°C: about 40% of maximal activity, glucoamylase
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycoside hydrolase family 31, GH31
additional information
isomaltose and panose docked at the active site of Aspergillus niger alpha-glucosidase involving the catalytic residues Asp490 and Asp660, putative nucleophile and acid/base catalytic residues, modelling, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AGLU_ASPNG
985
0
108913
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
alpha-glucosidases structure comparisons, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the wild-type enzyme contains over 35% more sugar than the recombinant enzyme
glycoprotein
glycoprotein
-
the intracellular enzyme contains 29 mol of mannose and 6 mol of glucosamine per mol of enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N694A
site-directed mutagenesis, the mutant shows altered transglucosylation activity compared to the wild-type
N694F
site-directed mutagenesis, the mutant shows altered transglucosylation activity compared to the wild-type, the pH optimum is increased compared to the wild-type enzyme
N694L
site-directed mutagenesis, the mutant shows altered transglucosylation activity compared to the wild-type, the pH optimum is increased and the thermal stability slightly reduced compared to the wild-type enzyme
N694W
site-directed mutagenesis, the mutant shows altered transglucosylation activity compared to the wild-type
additional information
additional information
construction of a gene constructs in which the aglA gene is fused to glycosylphosphatidylinositol anchor sequences, from the yeast SED1 gene, that determine the covalent binding of the hybrid protein to the cell membrane, for that yeast cells can be used directly as the catalytic agent to produce isomaltooligosaccharides (IMOs). The resulting hybrid enzymes are stably attached to the cell surface. The cells from cultures of recombinant yeast strains expressing aglA-SED1 constructions can be used to produce IMOs in successive batches
additional information
enzyme immobilization onto an epoxy-activated resin (Eupergit C), improved synthesis of isomaltooligosaccharides (IMOs) using immobilized alpha-glucosidase in organic-aqueous media, method optimization, overview. An immobilization efficiency of 79.61% is obtained under the condition of pH 6.0, ionic strength of 2.0 M, and 30 mg of protein/g of resin. The butyl acetate-aqueous biphasic system significantly improves the catalytic activity of the immobilized enzyme and the yield of IMOs. The highest yield of IMOs (50.83% w/w) is obtained at pH 4.5 and 55°C in a butyl acetate/buffer system (25:75 v/v)
additional information
preparation of the AglU-displaying Pichia pastoris whole-cell biocatalyst for optimized synthesis of isomaltooligosaccharides (IMOs). IMOs are a mixture that includes isomaltose (IG2), panose (P), and isomaltotriose (IG3). The recombinant Aspergillus niger enzyme expressed from Pichia pastoris has a high reaction efficiency and operational stability, method optimization and evaluation, overview. IMOs synthesis by transglycosylation, best at pH 4.0 and 55-60°C
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50% remaining activity after 72 h at 50°C, 50% remaining activity after 3 h at 60°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 15 days, 41% loss of maltase activity, 21% loss of glucoamylase activity
-
4°C, 15 days, 21% loss of maltase activity, 46% loss of glucoamylase activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme and recombinant secreted extracellular enzyme from Emericella nidulans strain JCM10259 by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration to homogeneity
recombinant His-tagged wild-type and mutant enzymes from Pichia pastoris by nickel affinity chromatography
ultrafiltration, ethanol fraction and hydrophobic interaction chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aglA, overexpression of the extracellular enzyme in Emericella nidulans strain JCM10259
gene aglA, recombinant expression in Saccharomyces cerevisiae strain BY474, which lacks maltose, under control of a galactose-inducible promoter. Recombinant yeast cells expressing the aglA gene produce extracellular alpha-glucosidase activity about half of which appeared cell bound whereas the other half is released into the culture medium
gene Agl, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Pichia pastoris
gene aglU, recombinant expression from plasmid pKANGL-GCW61 in Pichia pastoris strain GS115, cell surface display, recombinant expression in Escherichia coli TOP10 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
target for therapy of type 2 diabetes, antitumor activites, antiviral activites
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brizova, K.; Kralova, B.; Demnerova, K.
Isolation and characterization of alpha-glucosidase from Aspergillus niger
J. Chromatogr.
593
125-131
1992
Aspergillus niger, Saccharomyces cerevisiae, Wickerhamomyces anomalus, Penicillium brevicompactum, Penicillium citrinum, Schizosaccharomyces pombe
Rudick, M.J.; Fitzgerald, Z.E.; Rudick, V.L.
Intra- and extracellular forms of alpha-glucosidase from Aspergillus niger
Arch. Biochem. Biophys.
193
509-520
1979
Aspergillus niger
Kita, A.; Matsui, H.; Somoto, A.; Kimura, A.; Takata, M.; Chiba, S.
Substrate specificity and subsite affinities of crystalline alpha-glucosidase from Aspergillus niger
Agric. Biol. Chem.
55
2327-2335
1991
Aspergillus niger
-
Duan, K.J.; Sheu, D.C.; Lin, C.T.
Transglucosylation of a fungal alpha-glucosidase. The enzyme properties and correlation of isomaltooligosaccharide production
Ann. N. Y. Acad. Sci.
750
325-328
1995
Aspergillus niger
Hakamata, W.; Muroi, M.; Kadokura, K.; Nishio, T.; Oku, T.; Kimura, A.; Chiba, S.; Takatsuki, A.
Aglycon specificity profiling of alpha-glucosidases using synthetic probes
Bioorg. Med. Chem. Lett.
15
1489-1492
2005
Apis mellifera, Aspergillus niger, Geobacillus stearothermophilus, Beta vulgaris, Saccharomyces cerevisiae, Oryza sativa, Rattus norvegicus, Zea mays subsp. mays
Ogawa, M.; Nishio, T.; Minoura, K.; Uozumi, T.; Wada, M.; Hashimoto, N.; Kawachi, R.; Oku, T.
Recombinant alpha-glucosidase from Aspergillus niger. Overexpression by Emericella nidulans, purification and characterization
J. Appl. Glycosci.
53
13-16
2006
Aspergillus niger (P56526), Aspergillus niger GN-3 (P56526)
-
Hakamata, W.; Kurihara, M.; Okuda, H.; Nishio, T.; Oku, T.
Design and screening strategies for alpha-glucosidase inhibitors based on enzymological information
Curr. Top. Med. Chem.
9
3-12
2009
Apis mellifera, Aspergillus niger, Geobacillus stearothermophilus, Beta vulgaris, Saccharomyces cerevisiae, Oryza sativa, Zea mays, Saccharolobus solfataricus (P0CD66)
Chen, D.L.; Tong, X.; Chen, S.W.; Chen, S.; Wu, D.; Fang, S.G.; Wu, J.; Chen, J.
Heterologous expression and biochemical characterization of alpha-glucosidase from Aspergillus niger by Pichia pastroris
J. Agric. Food Chem.
58
4819-4824
2010
Aspergillus niger (A2QJF7), Aspergillus niger
Casa-Villegas, M.; Marin-Navarro, J.; Polaina, J.
Synthesis of isomaltooligosaccharides by Saccharomyces cerevisiae cells expressing Aspergillus niger alpha-glucosidase
ACS omega
2
8062-8068
2017
Aspergillus niger (P56526)
Ma, M.; Okuyama, M.; Sato, M.; Tagami, T.; Klahan, P.; Kumagai, Y.; Mori, H.; Kimura, A.
Effects of mutation of Asn694 in Aspergillus niger alpha-glucosidase on hydrolysis and transglucosylation
Appl. Microbiol. Biotechnol.
101
6399-6408
2017
Aspergillus niger (A0PCH8)
Wang, J.; Li, W.; Niu, D.; Singh, S.; Lu, F.; Liu, X.
Improved synthesis of isomaltooligosaccharides using immobilized alpha-glucosidase in organic-aqueous media
Food Sci. Biotechnol.
26
731-738
2017
Aspergillus niger (A0PCH8)
EXTERNAL LINKS (specific for EC-Number 3.2.1.20)
Transporter Classification Database (TCDB): 8.A.9.2.3
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