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Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase and Organism(s) Aspergillus awamori and UniProt Accession Q12537
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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: Aspergillus awamori
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
GA
GAI
-
-
-
-
GAII
-
-
-
-
gamma-amylase
Glucan 1,4-alpha-glucosidase
-
-
-
-
glucoamylase
glucose amylase
-
-
-
-
lysosomal alpha-glucosidase
-
-
-
-
Meiotic expression upregulated protein 17
-
-
-
-
amyloglucosidase
-
-
-
-
exo-1,4-alpha-glucosidase
-
-
-
-
gamma-amylase
-
-
-
-
glucoamylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
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
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
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
-
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
isomaltose + H2O
glucose
-
-
-
-
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
-
-
?
dextrin + 6 H2O
7 D-glucose
-
the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
dextrin + 6 H2O
7 D-glucose
-
potato dextrin, the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme hydrolyzes glucosidic bonds in amylase, amylopectin, and maltoligosaccharides
-
-
?
starch + H2O
glucose + ?
-
300fold preference for the alpha-1,4-glucosidic linkage over the alpha-1,6-glucosidic linkage
-
-
?
starch + H2O
glucose + ?
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
additional information
?
-
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
additional information
?
-
-
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
additional information
?
-
-
the hydrolysis reaction successively cleaves glucose residues from the nonreducing ends of starch, glycogen, and maltooligosaccharides
-
-
?
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
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
dextrin + 6 H2O
7 D-glucose
-
the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
additional information
?
-
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
additional information
?
-
-
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
maltoheptaose
-
wild-type enzyme or mutant enzymes Gly183Lys or S184H
0.25
maltotriose
-
recombinant enzyme expressed in Saccharomyces cerevisiae
additional information
additional information
-
Km-values for the wild type enzyme and the mutant enzymes V181T/N182Y/G183A, P307A/T310V/Y312M/N313G and V181T/N182Y/G183A/P307A/T310V/Y312M/N313G
-
additional information
additional information
-
0.333 mg/ml for maltose
-
additional information
additional information
-
Km-values for C320A/E400C and the cysteinesulfinic acid derivative of C320A/E400C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30.9
maltotriose
-
recombinant enzyme expressed in Saccharomyces cerevisiae
additional information
additional information
-
turnover numbers for C320A/E400C and the cysteinesulfinic acid derivative of C320A/E400C
-
additional information
additional information
-
turnover numbers for the wild-type enzyme and the mutant enzymes V181T/N182Y/G183A, P307A/T310V/Y312M/N313G and V181T/N182Y/G183A/P307A/T310V/Y312M/N313G
-
additional information
additional information
-
turnover numbers for the recombinant enzymes with maltose through maltoheptaose as substrates
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
values between 0.56 to 1.02 U/ml for different transformants
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
-
native glucoamylase, approx. 20% of maximal activity at pH 2.0 and pH 6.0, respectively, immobilized glucoamylase, approx. 30% of maximal activity at pH 2.0, approx. 40% of maximal activity at pH 6.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
65
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 75
-
immobilized glucamylase, approx. 20% of maximal activity at 30°C, approx. 50% of maximal activity at 75°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
significant glucoamylase activity is detected specifically in the seeds but not other tissues of the transgenic rice lines
additional information
-
significant glucoamylase activity is detected specifically in the seeds but not other tissues of the transgenic rice lines
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). Q12537_ASPAW
639
0
68278
TrEMBL
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
82327
-
x * 82327, mass spectroscopy, recombinant GA expressed in Pichia pastoris
82330
-
recombinant enzyme expressed in Pichia pastoris, matrix-assisted laser desorption ionization mass spectrometry
82839
-
x * 82839, mass spectroscopy, recombinant GA expressed in Aspergillus niger
83869
-
x * 83869, mass spectroscopy, recombinant GA expressed in Saccharomyces cerevisiae
83870
-
recombinant enzyme expressed in Saccharomyces cerevisiae, matrix-assisted laser desorption ionization mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 82327, mass spectroscopy, recombinant GA expressed in Pichia pastoris
?
-
x * 82839, mass spectroscopy, recombinant GA expressed in Aspergillus niger
?
-
x * 83869, mass spectroscopy, recombinant GA expressed in Saccharomyces cerevisiae
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
-
acid proteinases are involved in generating multiple glucoamylase forms in the fungus Aspergillus awamori through limited hydrolysis of this enzyme decreasing the stability of the enzyme in a pH-dependent manner, methods for removal of proteolytic activity, overview
glycoprotein
-
two N-linked and about forty short mannose-bearing O-linked sugars per molecule. O-linked sugars essentially contribute to the stabilization of glucoamylase domains
glycoprotein
-
glycosyl chains of 5 and 8 sugar residues are linked to Asp171 and Asp395 respectively
glycoprotein
-
deglycosylation of the enzyme leads to reduced thermal stability and a decrease in enzyme secretion, O-glycosylation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A246C
E400C
G127A/P128A
-
site-directed mutagenesis, the mutation decreases the enzyme thermostability compared to the wild-type protein
G137A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G139A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G183K
-
slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
I136L
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
P128A/G139A/I136L
-
site-directed mutagenesis, mutations G139A and I136L, located in the center of alpha-helix, completely compensate for the destabilization caused by substitution P128A
P307A/T310V/Y312M/N313G
-
up to 15fold decreased turnover-number for alpha-1,4-linked substrates. Up to 9fold increase in Km-value for alpha-1,6-linked substrates
S119Y
-
slight increase in activity as compared with the wild-type enzyme towards maltose. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S184H
-
slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S411A
-
54-74% of the catalytic efficiency of the wild type enzyme. Increased pH-optimum by 0.8 units for both maltose and maltoheptaose hydrolysis while maintaining a high level of activity and catalytic efficiency. In hydrolysis of 28% DE 10 maltodextrin, the mutant enzyme has a pH optimum of 7 compared with 5.6 for wild-type enzyme, and has higher initial rates of glucose production than wild-type enzyme at all pH values tested above pH 6.6
S411G
-
catalytic efficiency like that of wild type enzyme for isomaltose, maltose and maltoheptaose hydrolysis at pH 4.4
S54P/T314A/H415Y
-
the mutant enzyme is more thermostable compared to the wild-type enzyme at 70°C. The mutation does not affect the protein secretion nor the production of the enzyme
V181T/N182Y/G183A
-
2fold increased Km-value for alpha-1,4-linked substrates: For alpha-1,6-linked substrates a 2fold increase in Km and a 3fold decrease in turnover-number
V181T/N182Y/G183A/P307A/T310V/Y312M/A313G
-
remarkably low Km-value for isomaltotriose through isomaltoheptaose and elevated turnover-number on isomaltose, resulting in an approximately 2fold improved catalytic effeciency
additional information
A246C
-
the T50-value is enhanced by 4°C to 73°C. Compared to wild-type enzyme, the mutant is twice as active at 66°C but half as active at 45°C
A246C
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
E400C
-
cysteinesulfinic acid derivative of C320A/E400C-SO2H has a 700times higher turnover number towards maltose relative to C320A/E400C, while the Km-value is unchanged. Compared to wild-type enzyme, the C400-SO2H derivative has a turnover number of 150-190% and 85-320% on maltooliogosaccharides and isomaltooligosaccharides respectively, while Km-values are similar to that of wild-type for disaccharides and 3.5-5.5fold and 1.8-2.5fold higher for the longer maltooligosaccharides and isomaltooligosaccharides. The inhibition constant of cysteinesulfinic acid derivative of C320A/E400C-SO2H for acarbose increases more than 10000-fold
E400C
-
further oxidation of Cys thiol group to sulfinic acid, up to 300% higher kcat and decreased Km compared to wild-type, depending on substrate
additional information
-
the enzyme from commercial preparation is immobilized by sorption on a carbon support Sibunit, starch and dextrin hydrolysis kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, show that immobilization of the enzyme results in a 1000fold increase in enzyme stability in comparison to the dissolved enzyme, presence of the dextrin substrate has a stabilizing effect, increase in dextrin concentration to 53% increases the thermostability of the immobilized enzyme, the immobilized-enzyme biocatalyst for starch saccharification has a high operational stability, half-inactivation time at 60°C exceeds 30 days, method optimization, overview
additional information
-
the enzyme immobilized on foamed glass covered with the catalytic filament carbon layer is highly active and stable, the effect of the carbon layer synthesized on the surface of aluminum oxide on the properties of biocatalysts shows that the glucoamylase adsorbed on the carbon-containing mesoporous ny-aluminum oxide exhibits a greater activity than the glucoamylase adsorbed on the macroporous alpha-aluminum oxide, kinetics, overview
additional information
-
molecular construction, molecular modeling and molecular dynamics of engineered enzyme with higher thermostability through optimized intrinsic interactions within alpha-helix D, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
-
the recombinant enzyme mutant S54P/T314A/H415Y retains 80% of its activity within this range
717107
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
freshly isolated purified commercial preparation, 10 h, loss of 50% activity, purified commercial preparation after 6 months of storage, 10 h, loss of 75% activity
55
-
freshly isolated purified commercial preparation, 10 h, loss of over 80% activity, purified commercial preparation after 6 months of storage, 10 h, loss of over 90% activity
60
-
purified recombinant enzyme mutant S54P/T314A/H415Y, stable up to, irreversible thermo-inactivation of the mutant enzyme follows first-order kinetics
65
-
purified recombinant enzyme mutant S54P/T314A/H415Y, half-life is 76 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
modification of the carbohydrate component by adding 1-deoxymannonojirimycin to the culture medium induces inhibition of alpha-mannosidase involved in the processing, leading to a more complete glycosylation and consequently to a higher stability of the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
5°C, half-life 6 days in absence of protease inhibitor, in presence of protease inhibitor mixture the enzyme is stable for at least 1 year showing 95% remaining activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
further purification of the commercial preparation by anion exchange chromatography
-
recombinant enzyme mutant S54P/T314A/H415Y from Saccharomyces cerevisiae by acarbose affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris, Saccharomyces cerevisiae and Aspergillus niger
-
expression in Pichia pastoris, Saccharomyces cerevisiae or Aspergillus niger. In Pichia pastoris the C320A/E400C double mutant is produced at 75% of the wild-type glucoamylase, while the corresponding single mutants are produced at 1% and 20% of the wild-type level, respectively
-
expression of wild-type and mutant S54P/T314A/H415Y enzymes in Saccharomyces cerevisiae
-
expression of wild-type enzyme in Saccharomyces cerevisiae strain C468, cloning and expression of mutant enzymes in Escherichia coli strain DH5alpha
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
industry
an important industrial enzyme used in starch enzymatic saccharification
synthesis
-
preparations of glucoamylase are widely used in many branches of industry for hydrolyzing starch-containing raw materials
biotechnology
-
the enzyme from commercial preparation is immobilized by sorption on a carbon support Sibunit, starch and dextrin hydrolysis kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, show that immobilization of the enzyme results in a 1000fold increase in enzyme stability in comparison to the dissolved enzyme, presence of the dextrin substrate has a stabilizing effect, increase in dextrin concentration to 53% increases the thermostability of the immobilized enzyme, the immobilized-enzyme biocatalyst for starch saccharification has a high operational stability, half-inactivation time at 60°C exceeds 30 days
biotechnology
-
the enzyme immobilized on foamed glass covered with the catalytic filament carbon layer is highly active and stable, the effect of the carbon layer synthesized on the surface of aluminum oxide on the properties of biocatalysts shows that the glucoamylase adsorbed on the carbon-containing mesoporous ny-aluminum oxide exhibits a greater activity than the glucoamylase adsorbed on the macroporous alpha-aluminum oxide, kinetics, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nunberg, J.H.; Meade, J.H.; Cole, G.; Lawyer, F.C.; McCabe, P.; Schweickart, V.; Tal, R.; Wittman, V.P.; Flatgaard, J.E.; Innis, M.A.
Molecular cloning and characterization of the glucoamylase gene of Aspergillus awamori
Mol. Cell. Biol.
4
2306-2315
1984
Aspergillus awamori
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
Yamasaki, Y.; Suzuki, Y.; Ozawa, J.
Three forms of alpha-glucosidase and a glucoamylase from Aspergillus awamori
Agric. Biol. Chem.
41
2149-2161
1977
Aspergillus awamori
-
Aleshin, A.E.; Hoffman, C.; Firsov, L.M.; Honzatko, R.B.
Refined crystal structures of glucoamylase from Aspergillus awamori var. X100
J. Mol. Biol.
13; 238
575-591
1994
Aspergillus awamori
Golubev, A.M.; Neustroev, K.N.; Aleshin, A.E.; Firsov, L.M.
Crystallization and preliminary X-ray study of minor glucoamylase from Aspergillus awamori variant X-100/D27
J. Mol. Biol.
226
271-272
1992
Aspergillus awamori
Fang, T.Y.; Ford, C.
Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum
Protein Eng.
11
383-388
1998
Aspergillus awamori
Neustroev, K.N.; Golubev, A.M.; Firsov, L.M.; Ibatullin, F.M.; Protasevich, I.I.; Makarov, A.A.
Effect of modification of carbohydrate component on properties of glucoamylase
FEBS Lett.
316
157-160
1993
Aspergillus awamori
Fierobe, H.P.; Clarke, A.J.; Tull, D.; Svensson, B.
Enzymatic properties of the cysteinesulfinic acid derivative of the catalytic-base mutant Glu400->Cys of glucoamylase from Aspergillus awamori
Biochemistry
37
3753-3759
1998
Aspergillus awamori
Fierobe, H.P.
Mutational modulation of substrate bond-type specificity and thermostability of glucoamylase from Aspergillus awamori by replacement with short homologue active site sequences and thiol/disulfide engineering
Biochemistry
35
8696-8704
1996
Aspergillus awamori
Fierobe, H.P.; Mirgorodskaya, E.; Frandsen, T.P.; Roepstorff, P.; Svensson, B.
Overexpression and characterization of Aspergillus awamori wild-type and mutant glucoamylase secreted by the methylotrophic yeast Pichia pastoris: comparison with wild-type recombinant glucoamylase produced using Saccharomyces cerevisiae and Aspergillus niger as hosts
Protein Expr. Purif.
9
159-170
1997
Aspergillus awamori
Sierks, M.R.; Svennson, B.
Protein engineering of the relative specificity of glucoamylase from Aspergillus awamori based on sequence similarities between starch degrading enzymes
Protein Eng.
7
1479-1484
1994
Aspergillus awamori
Ruadze, I.D.; Zherebtsov, N.A.; Slepokurova, Y.I.; Selemenev, V.F.; Shkutina, I.V.; Stoyanova, O.F.
Preparation and characterization of immobilized Aspergillus awamori 466 glucoamylase
Appl. Biochem. Microbiol.
37
178-183
2001
Aspergillus awamori, Aspergillus awamori 466
-
Sauer, J.; Sigurskjold, B.W.; Christensen, U.; Frandsen, T.P.; Mirgorodskaya, E.; Harrison, M.; Roepstorff, P.; Svensson, B.
Glucoamylase: structure/function relationships, and protein engineering
Biochim. Biophys. Acta
1543
275-293
2000
Aspergillus awamori, Aspergillus niger, Saccharomycopsis fibuligera
Liu, H.L.; Doleyres, Y.; Coutinho, P.M.; Ford, C.; Reilly, P.J.
Replacement and deletion mutations in the catalytic domain and belt region of Aspergillus awamori glucoamylase to enhance thermostability
Protein Eng.
13
655-659
2000
Aspergillus awamori
Liu, H.L.; Wang, W.C.
Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations
Protein Eng.
16
19-25
2003
Aspergillus awamori (P69327), Aspergillus awamori
Frater, T.; Nemestothy, N.; Gubicza, L.; Belafi-Bako, K.
Enhancement of operation and storage stability of glucoamylase from Aspergillus awamori by a protease inhibitor preparation
Biocatal. Biotransform.
23
281-284
2005
Aspergillus awamori
-
Norouzian, D.; Akbarzadeh, A.; Scharer, J.M.; Moo Young, M.
Fungal glucoamylases
Biotechnol. Adv.
24
80-85
2005
Aspergillus awamori, Aspergillus foetidus, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus terreus, Mucor javanicus, Neurospora crassa, Rhizopus arrhizus, Rhizopus niveus, Rhizopus microsporus var. oligosporus, Mycothermus thermophilus, Trichoderma reesei, Mucor rouxians, Arthrobotrys amerospora, Monascus kaoliang, Monascus kaoliang F-1, Aspergillus awamori X-100, Aspergillus terreus NA-170, Aspergillus niger NRRL 330, Aspergillus terreus NA-770
Kovalenko, G.A.; Perminova, L.V.; Plaksin, G.V.; Chuenko, T.V.; Komova, O.V.; Rudina, N.A.
Immobilized glucoamylase: A biocatalyst of dextrin hydrolysis
Appl. Biochem. Microbiol.
42
145-149
2006
Aspergillus awamori
-
Rakhimova, N.M.; Khasanov, K.T.; Davranov, K.D.
The effect of acid proteinases on the activity and stability of glucoamylase preparations
Appl. Biochem. Microbiol.
42
181-185
2006
Aspergillus awamori
-
Kovalenko, G.A.; Perminova, L.V.; Terenteva, T.G.; Plaksin, G.V.
Catalytic properties of glucoamylase immobilized on synthetic carbon material Sibunit
Appl. Biochem. Microbiol.
43
374-378
2007
Aspergillus awamori
-
Xu, X.; Huang, J.; Fang, J.; Lin, C.; Cheng, J.; Shen, Z.
Expression of a fungal glucoamylase in transgenic rice seeds
Protein Expr. Purif.
61
113-116
2008
Aspergillus awamori (P69327), Aspergillus awamori
Kim, J.H.; Kim, H.R.; Lim, M.H.; Ko, H.M.; Chin, J.E.; Lee, H.B.; Kim, I.C.; Bai, S.
Construction of a direct starch-fermenting industrial strain of Saccharomyces cerevisiae producing glucoamylase, alpha-amylase and debranching enzyme
Biotechnol. Lett.
32
713-719
2010
Aspergillus awamori
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)
Pavezzi, F.C.; Carneiro, A.A.; Bocchini-Martins, D.A.; Alves-Prado, H.F.; Ferreira, H.; Martins, P.M.; Gomes, E.; da Silva, R.
Influence of different substrates on the production of a mutant thermostable glucoamylase in submerged fermentation
Appl. Biochem. Biotechnol.
163
14-24
2011
Aspergillus awamori, Aspergillus awamori C468
Surzhik, M.; Churkina, S.; Shmidt, A.; Shvetsov, A.; Kozhina, T.; Firsov, D.; Firsov, L.; Petukhov, M.
The effect of point amino acid substitutions in an internal alpha-helix on thermostability of Aspergillus awamori X100 glucoamylase
Appl. Biochem. Microbiol.
46
206-211
2010
Aspergillus awamori, Aspergillus awamori X100
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