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Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P04065
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EC Tree
3.2.1.3 glucan 1,4-alpha-glucosidaseIUBMB 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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Word Map
- 3.2.1.3
- aspergillus
- niger
- glycogen
- alpha-amylase
- maltose
- corn
- awamori
-
amylolytic
- pompe
- sucrase
- myopathy
-
saccharification
- rhizopus
- lactase
-
brush
- sucrase-isomaltase
- acarbose
- dextrin
- glycogenosis
- maltotriose
- amylopectin
- flour
- amylases
-
starch-binding
- isomaltase
-
infantile
- maltodextrins
- occidentalis
- bran
- disaccharidase
- food industry
- pullulanase
-
liquefaction
- beta-cyclodextrins
-
debranching
- beta-amylase
-
carbohydrases
-
3.2.1.20
- cassava
- maltooligosaccharides
- trehalase
-
saccharify
-
bioethanol
- medicine
- industry
- energy production
- paper production
-
glucanotransferase
- nutrition
- maltoheptaose
- analysis
- maltotetraose
- biotechnology
- cgtase
- biofuel production
- isoamylase
-
liquefied
- 1-deoxynojirimycin
-
starchy
- synthesis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
glucoamylase, amyloglucosidase, acid maltase, maltase-glucoamylase, lysosomal alpha-glucosidase, maltase glucoamylase, gamma-amylase, glucose amylase, gam-1, glucoamylase p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-alpha-D-glucan glucohydrolase
-
-
-
-
acid maltase
-
-
-
-
alpha-1,4-glucan glucohydrolase
-
-
-
-
amyloglucosidase
-
-
-
-
exo-1,4-alpha-glucosidase
-
-
-
-
GAI
-
-
-
-
GAII
-
-
-
-
gamma-amylase
-
-
-
-
Glucan 1,4-alpha-glucosidase
-
-
-
-
glucoamylase
glucose amylase
-
-
-
-
lysosomal alpha-glucosidase
-
-
-
-
Meiotic expression upregulated protein 17
-
-
-
-
glucoamylase
-
-
-
-
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
9032-08-0
-
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
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme plays a role in the saccharification and fermentation of amylaceous substrates, notably in high cell density processes
-
-
?
additional information
?
-
-
no hydrolysis of alpha-1,6 linkages
-
-
?
additional information
?
-
-
no hydrolysis of alpha-1,6 linkages
-
-
?
additional information
?
-
-
glucoamylase is an exoglycosidase responsible for hydrolyzing the terminal alpha-1,4 glucosidic bonds of dextrins and related oligo- and polysaccharides, the reaction involves a proton transfer by acid catalysis, followed by formation of a transition state analogous to an oxocarbonium ion, and finally, a base-catalyzed nucleophilic attack of water, glutamic acid present in different regions of the enzyme-active site acts as the acid and base catalysts required for the reaction
-
-
?
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
starch + H2O
D-glucose + ?
-
the enzyme plays a role in the saccharification and fermentation of amylaceous substrates, notably in high cell density processes
-
-
?
additional information
?
-
-
glucoamylase is an exoglycosidase responsible for hydrolyzing the terminal alpha-1,4 glucosidic bonds of dextrins and related oligo- and polysaccharides, the reaction involves a proton transfer by acid catalysis, followed by formation of a transition state analogous to an oxocarbonium ion, and finally, a base-catalyzed nucleophilic attack of water, glutamic acid present in different regions of the enzyme-active site acts as the acid and base catalysts required for the reaction
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
biphasic kinetics for maltodextrin degradation
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
fermentation activity of diverse commercial enzyme samples, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cell culture growth conditions, optimization, partition factors, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the extracellular enzyme is attached to the cell wall
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the replacement of native beta-glucosidase Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
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). AMYH_YEASX
767
1
82489
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
glucoamylase is a two-domain protein composed by a N-terminal serinethreonine-rich domain and a C-terminal domain with the typical structure of the catalytic domain of fungal glucoamylases
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
construction of a series of hybrid enzymes by interchanging domains of glucoamylase Sta1 from Saccharomyces cerevisiae and beta-glucosidase Bgl1 from Saccharomycopsis fibuligera strain ATCC 9947 based on the homology-based structural models of the two proteins. The replacement of native Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
energy production
-
the enzyme is useful in fuel ethanol production, enzyme properties and performance, overview
industry
-
glucoamylases have been used with alpha-amylases for the industrial conversion of starch into glucose, intact cells of thermotolerant yeasts can be used as colloidal biocatalysts in starch degradation processes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pugh, T.A.; Shah, J.C.; Magee, P.T.; Calncy, M.J.
Characterization and localization of the sporulation glucoamylase of Saccharomyces cerevisiae
Biochim. Biophys. Acta
994
200-209
1989
Saccharomyces cerevisiae
Kleinman, M.J.; Wilkinson, A.E.; Wright, I.P.; Evans, I.H.; Bevan, E.A.
Purification and properties of an extracellular glucoamylase from a diastatic strain of Saccharomyces cerevisiae
Biochem. J.
249
163-170
1988
Aspergillus oryzae, Saccharomyces cerevisiae, Rhizopus sp., Saccharomyces cerevisiae 1ab
Saville, B.A.; Huang, C.; Yacyshyn, V.; Desbarats, A.
Properties and performance of glucoamylases for fuel ethanol production
Appl. Biochem. Biotechnol.
129-132
180-194
2006
Saccharomyces cerevisiae
Peres, M.F.; Souza, C.S.; Thomaz, D.; de Souza, A.R.; Laluce, C.
Partitioning of the glucoamylase activity at the cell surfaces in cultures of Saccharomyces
Process Biochem.
41
20-27
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae 'var. diastaticus'
-
Kumar, P.; Satyanarayana, T.
Microbial glucoamylases: characteristics and applications
Crit. Rev. Biotechnol.
29
225-255
2009
Aspergillus fumigatus, Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus sp., Aspergillus terreus, Aureobasidium pullulans, Saccharomyces cerevisiae, Moesziomyces antarcticus, Cephalosporium eichhorniae, Thermochaetoides thermophila, Thermoanaerobacter thermohydrosulfuricus, Thermoanaerobacterium thermosaccharolyticum, Curvularia lunata, Saccharomycopsis fibuligera, Endomycopsis fibuligera, Fusarium solani, Thermomyces lanuginosus, Humicola sp., Monascus sp. (in: Fungi), Mucor circinelloides, Mucor javanicus, Neurospora crassa, Paecilomyces variotii, Rhizopus arrhizus, Rhizopus sp., Saccharomyces cerevisiae 'var. diastaticus', Schwanniomyces castellii, Mycothermus thermophilus, Saccharolobus solfataricus, Thermoplasma acidophilum, Trichoderma reesei, Lactobacillus amylovorus, Thielaviopsis paradoxa, Thermomucor indicae-seudaticae, Picrophilus torridus, Arthrobotrys amerospora, Lentinula edodes L-54, Aspergillus awamori (Q12537)
Kilonzo, P.M.; Margaritis, A.; Bergougnou, M.A.
Plasmid stability and kinetics of continuous production of glucoamylase by recombinant Saccharomyces cerevisiae in an airlift bioreactor
J. Ind. Microbiol. Biotechnol.
36
1157-1169
2009
Saccharomyces cerevisiae
Marin-Navarro, J.; Gurgu, L.; Alamar, S.; Polaina, J.
Structural and functional analysis of hybrid enzymes generated by domain shuffling between Saccharomyces cerevisiae (var. diastaticus) Sta1 glucoamylase and Saccharomycopsis fibuligera Bgl1 beta-glucosidase
Appl. Microbiol. Biotechnol.
89
121-130
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
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