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Literature summary for 3.2.1.3 extracted from

  • Norouzian, D.; Akbarzadeh, A.; Scharer, J.M.; Moo Young, M.
    Fungal glucoamylases (2005), Biotechnol. Adv., 24, 80-85.
    View publication on PubMed

Application

Application Comment Organism
industry Rhizopus enzymes are useful in industrial applications Rhizopus arrhizus
industry the enzyme is useful in industrial applications Aspergillus niger
industry the enzyme is useful in industrial applications Aspergillus oryzae
industry the enzyme is useful in industrial applications Aspergillus phoenicis
industry the enzyme is useful in industrial applications Rhizopus niveus
industry the enzyme is useful in industrial applications Rhizopus microsporus var. oligosporus

Protein Variants

Protein Variants Comment Organism
additional information improvement of enzyme for inductrial applications Aspergillus niger
additional information improvement of enzyme for inductrial applications Rhizopus arrhizus
additional information improvement of enzyme for industrial applications Rhizopus niveus

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall the enzyme is adsorbed to the cell wall Neurospora crassa 5618
-
cell wall the enzyme is adsorbed to the cell wall Aspergillus niger 5618
-
cell wall the enzyme is adsorbed to the cell wall Rhizopus arrhizus 5618
-
cell wall the enzyme is adsorbed to the cell wall Aspergillus oryzae 5618
-
cell wall the enzyme is adsorbed to the cell wall Aspergillus terreus 5618
-
cell wall the enzyme is adsorbed to the cell wall Trichoderma reesei 5618
-
cell wall the enzyme is adsorbed to the cell wall Aspergillus awamori 5618
-
cell wall the enzyme is adsorbed to the cell wall Rhizopus niveus 5618
-
cell wall the enzyme is adsorbed to the cell wall Mucor javanicus 5618
-
cell wall the enzyme is adsorbed to the cell wall Aspergillus foetidus 5618
-
cell wall the enzyme is adsorbed to the cell wall Mycothermus thermophilus 5618
-
cell wall the enzyme is adsorbed to the cell wall Mucor rouxians 5618
-
cell wall the enzyme is adsorbed to the cell wall Arthrobotrys amerospora 5618
-
cell wall the enzyme is adsorbed to the cell wall Monascus kaoliang 5618
-
extracellular
-
Neurospora crassa
-
-
extracellular
-
Aspergillus niger
-
-
extracellular
-
Rhizopus arrhizus
-
-
extracellular
-
Aspergillus oryzae
-
-
extracellular
-
Aspergillus terreus
-
-
extracellular
-
Aspergillus phoenicis
-
-
extracellular
-
Trichoderma reesei
-
-
extracellular
-
Aspergillus awamori
-
-
extracellular
-
Rhizopus niveus
-
-
extracellular
-
Mucor javanicus
-
-
extracellular
-
Aspergillus foetidus
-
-
extracellular
-
Rhizopus microsporus var. oligosporus
-
-
extracellular
-
Mycothermus thermophilus
-
-
extracellular
-
Mucor rouxians
-
-
extracellular
-
Arthrobotrys amerospora
-
-
extracellular
-
Monascus kaoliang
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
125000
-
-
Aspergillus niger

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
starch + H2O Neurospora crassa 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 beta-D-glucose + ?
-
?
starch + H2O Aspergillus niger 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 beta-D-glucose + ?
-
?
starch + H2O Rhizopus arrhizus 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 beta-D-glucose + ?
-
?
starch + H2O Aspergillus oryzae 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 beta-D-glucose + ?
-
?
starch + H2O Aspergillus terreus 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 beta-D-glucose + ?
-
?
starch + H2O Trichoderma reesei 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 beta-D-glucose + ?
-
?
starch + H2O Aspergillus awamori 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 beta-D-glucose + ?
-
?
starch + H2O Rhizopus niveus 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 beta-D-glucose + ?
-
?
starch + H2O Mucor javanicus 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 beta-D-glucose + ?
-
?
starch + H2O Aspergillus foetidus 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 beta-D-glucose + ?
-
?
starch + H2O Mycothermus thermophilus 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 beta-D-glucose + ?
-
?
starch + H2O Mucor rouxians 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 beta-D-glucose + ?
-
?
starch + H2O Arthrobotrys amerospora 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 beta-D-glucose + ?
-
?
starch + H2O Monascus kaoliang 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 beta-D-glucose + ?
-
?
starch + H2O Neurospora crassa the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus niger the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Rhizopus arrhizus the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus oryzae the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus terreus the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus phoenicis the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Trichoderma reesei the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus awamori the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Rhizopus niveus the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Mucor javanicus the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus foetidus the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Rhizopus microsporus var. oligosporus the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Mycothermus thermophilus the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Mucor rouxians the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Arthrobotrys amerospora the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Monascus kaoliang the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Monascus kaoliang F-1 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 beta-D-glucose + ?
-
?
starch + H2O Monascus kaoliang F-1 the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus awamori X-100 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 beta-D-glucose + ?
-
?
starch + H2O Aspergillus awamori X-100 the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus terreus NA-170 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 beta-D-glucose + ?
-
?
starch + H2O Aspergillus terreus NA-170 the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus niger NRRL 330 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 beta-D-glucose + ?
-
?
starch + H2O Aspergillus niger NRRL 330 the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?
starch + H2O Aspergillus terreus NA-770 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 beta-D-glucose + ?
-
?
starch + H2O Aspergillus terreus NA-770 the enzyme is required for degradation of raw starch starch + beta-D-glucose
-
?

Organism

Organism UniProt Comment Textmining
Arthrobotrys amerospora
-
-
-
Aspergillus awamori
-
-
-
Aspergillus awamori
-
var. kawachi
-
Aspergillus awamori X-100
-
-
-
Aspergillus foetidus
-
-
-
Aspergillus niger
-
-
-
Aspergillus niger
-
at least six isozymes, several strains, e.g. strain NRRL 330
-
Aspergillus niger NRRL 330
-
-
-
Aspergillus oryzae
-
-
-
Aspergillus phoenicis
-
-
-
Aspergillus terreus
-
-
-
Aspergillus terreus NA-170
-
-
-
Aspergillus terreus NA-770
-
-
-
Monascus kaoliang
-
two active forms
-
Monascus kaoliang
-
nov-sp. F-1
-
Monascus kaoliang F-1
-
two active forms
-
Mucor javanicus
-
-
-
Mucor rouxians
-
-
-
Mycothermus thermophilus
-
-
-
Neurospora crassa
-
-
-
Rhizopus arrhizus
-
-
-
Rhizopus microsporus var. oligosporus
-
-
-
Rhizopus niveus
-
-
-
Rhizopus niveus
-
isozymes glucoamylase C and D
-
Trichoderma reesei
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Aspergillus niger
glycoprotein
-
Rhizopus arrhizus
glycoprotein
-
Aspergillus oryzae
glycoprotein
-
Aspergillus terreus
glycoprotein
-
Trichoderma reesei
glycoprotein
-
Aspergillus awamori
glycoprotein
-
Mucor javanicus
glycoprotein
-
Aspergillus foetidus
glycoprotein
-
Mycothermus thermophilus
glycoprotein
-
Mucor rouxians
glycoprotein
-
Arthrobotrys amerospora
glycoprotein
-
Monascus kaoliang
glycoprotein O-glycosylation Rhizopus arrhizus
glycoprotein O-glycosylation Aspergillus oryzae
glycoprotein O-glycosylation Aspergillus terreus
glycoprotein O-glycosylation Aspergillus phoenicis
glycoprotein O-glycosylation Trichoderma reesei
glycoprotein O-glycosylation Mucor javanicus
glycoprotein O-glycosylation Aspergillus foetidus
glycoprotein O-glycosylation Rhizopus microsporus var. oligosporus
glycoprotein O-glycosylation Mycothermus thermophilus
glycoprotein O-glycosylation Mucor rouxians
glycoprotein O-glycosylation Arthrobotrys amerospora
glycoprotein O-glycosylation Monascus kaoliang
glycoprotein deglycosylation of the enzyme leads to reduced thermal stability and a decrease in enzyme secretion, O-glycosylation Aspergillus awamori
glycoprotein O-glycosylation, 5.1% carbohydrate content Neurospora crassa
glycoprotein O-glycosylation, isozymes glucoamylase C and D have 14.9% and 12.7% carbohydrate content, respectively Rhizopus niveus
glycoprotein O-glycosylation, required for enzyme stability and activity, structure overview Aspergillus niger
glycoprotein glucoamylase C and D contain 14.9% and 12.7% carbohydrate, respectively Rhizopus niveus
glycoprotein the enzyme contains 5.1% carbohydrate Neurospora crassa

Reaction

Reaction Comment Organism Reaction ID
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Neurospora crassa
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Aspergillus niger
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Rhizopus arrhizus
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Aspergillus oryzae
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Aspergillus terreus
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Aspergillus phoenicis
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Trichoderma reesei
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Aspergillus awamori
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Rhizopus niveus
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Mucor javanicus
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Aspergillus foetidus
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Rhizopus microsporus var. oligosporus
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Mycothermus thermophilus
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Mucor rouxians
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Arthrobotrys amerospora
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages Monascus kaoliang

Source Tissue

Source Tissue Comment Organism Textmining
additional information culture conditions for enzyme production, overview Aspergillus niger
-
additional information culture conditions for enzyme production, overview Rhizopus arrhizus
-
additional information culture conditions for enzyme production, overview Rhizopus niveus
-
additional information culture conditions for enzyme production, overview Rhizopus microsporus var. oligosporus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + H2O 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 Neurospora crassa beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus niger beta-D-glucose + ?
-
?
starch + H2O 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 Rhizopus arrhizus beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus oryzae beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus terreus beta-D-glucose + ?
-
?
starch + H2O 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 Trichoderma reesei beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus awamori beta-D-glucose + ?
-
?
starch + H2O 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 Rhizopus niveus beta-D-glucose + ?
-
?
starch + H2O 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 Mucor javanicus beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus foetidus beta-D-glucose + ?
-
?
starch + H2O 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 Mycothermus thermophilus beta-D-glucose + ?
-
?
starch + H2O 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 Mucor rouxians beta-D-glucose + ?
-
?
starch + H2O 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 Arthrobotrys amerospora beta-D-glucose + ?
-
?
starch + H2O 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 Monascus kaoliang beta-D-glucose + ?
-
?
starch + H2O 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 Neurospora crassa beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus niger beta-D-glucose + ?
-
?
starch + H2O 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 Rhizopus arrhizus beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus oryzae beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus terreus beta-D-glucose + ?
-
?
starch + H2O 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 Trichoderma reesei beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus awamori beta-D-glucose + ?
-
?
starch + H2O 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 Rhizopus niveus beta-D-glucose + ?
-
?
starch + H2O 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 Mucor javanicus beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus foetidus beta-D-glucose + ?
-
?
starch + H2O 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 Mycothermus thermophilus beta-D-glucose + ?
-
?
starch + H2O 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 Mucor rouxians beta-D-glucose + ?
-
?
starch + H2O 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 Arthrobotrys amerospora beta-D-glucose + ?
-
?
starch + H2O 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 Monascus kaoliang beta-D-glucose + ?
-
?
starch + H2O 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 Monascus kaoliang F-1 beta-D-glucose + ?
-
?
starch + H2O 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 Monascus kaoliang F-1 beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus awamori X-100 beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus awamori X-100 beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus terreus NA-170 beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus terreus NA-170 beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus niger NRRL 330 beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus niger NRRL 330 beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus terreus NA-770 beta-D-glucose + ?
-
?
starch + H2O 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 Aspergillus terreus NA-770 beta-D-glucose + ?
-
?
starch + H2O
-
Neurospora crassa starch + beta-D-glucose
-
?
starch + H2O
-
Rhizopus arrhizus starch + beta-D-glucose
-
?
starch + H2O
-
Aspergillus terreus starch + beta-D-glucose
-
?
starch + H2O
-
Trichoderma reesei starch + beta-D-glucose
-
?
starch + H2O
-
Aspergillus awamori starch + beta-D-glucose
-
?
starch + H2O
-
Rhizopus niveus starch + beta-D-glucose
-
?
starch + H2O
-
Mucor javanicus starch + beta-D-glucose
-
?
starch + H2O
-
Aspergillus foetidus starch + beta-D-glucose
-
?
starch + H2O
-
Rhizopus microsporus var. oligosporus starch + beta-D-glucose
-
?
starch + H2O
-
Mycothermus thermophilus starch + beta-D-glucose
-
?
starch + H2O
-
Mucor rouxians starch + beta-D-glucose
-
?
starch + H2O
-
Monascus kaoliang starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Neurospora crassa starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus niger starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Rhizopus arrhizus starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus oryzae starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus terreus starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus phoenicis starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Trichoderma reesei starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus awamori starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Rhizopus niveus starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Mucor javanicus starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus foetidus starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Rhizopus microsporus var. oligosporus starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Mycothermus thermophilus starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Mucor rouxians starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Arthrobotrys amerospora starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Monascus kaoliang starch + beta-D-glucose
-
?
starch + H2O the enzyme contains 7 subsites for substrate binding, subsite affinities Aspergillus niger starch + beta-D-glucose
-
?
starch + H2O the enzyme contains 7 subsites for substrate binding, subsite affinities Aspergillus oryzae starch + beta-D-glucose
-
?
starch + H2O the enzyme contains 7 subsites for substrate binding, subsite affinities Aspergillus phoenicis starch + beta-D-glucose
-
?
starch + H2O the enzyme contains 7 subsites for substrate binding, subsite affinities Arthrobotrys amerospora starch + beta-D-glucose
-
?
starch + H2O
-
Monascus kaoliang F-1 starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Monascus kaoliang F-1 starch + beta-D-glucose
-
?
starch + H2O
-
Aspergillus awamori X-100 starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus awamori X-100 starch + beta-D-glucose
-
?
starch + H2O
-
Aspergillus terreus NA-170 starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus terreus NA-170 starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus niger NRRL 330 starch + beta-D-glucose
-
?
starch + H2O the enzyme contains 7 subsites for substrate binding, subsite affinities Aspergillus niger NRRL 330 starch + beta-D-glucose
-
?
starch + H2O
-
Aspergillus terreus NA-770 starch + beta-D-glucose
-
?
starch + H2O the enzyme is required for degradation of raw starch Aspergillus terreus NA-770 starch + beta-D-glucose
-
?

Subunits

Subunits Comment Organism
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Neurospora crassa
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Rhizopus arrhizus
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Aspergillus terreus
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Trichoderma reesei
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Aspergillus awamori
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Rhizopus niveus
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Mucor javanicus
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Aspergillus foetidus
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Rhizopus microsporus var. oligosporus
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Mycothermus thermophilus
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Mucor rouxians
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus Monascus kaoliang
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding Aspergillus niger
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding Aspergillus oryzae
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding Aspergillus phoenicis
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding Arthrobotrys amerospora
More 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 Neurospora crassa
More 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 Aspergillus niger
More 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 Rhizopus arrhizus
More 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 Aspergillus oryzae
More 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 Aspergillus terreus
More 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 Trichoderma reesei
More 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 Aspergillus awamori
More 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 Rhizopus niveus
More 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 Mucor javanicus
More 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 Aspergillus foetidus
More 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 Mycothermus thermophilus
More 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 Mucor rouxians
More 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 Arthrobotrys amerospora
More fungal glucoamylases contain up to 7 subsites for substrate bindingwith 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 Rhizopus arrhizus
More fungal glucoamylases contain up to 7 subsites for substrate bindingwith 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 Monascus kaoliang

Synonyms

Synonyms Comment Organism
amyloglucosidase
-
Neurospora crassa
amyloglucosidase
-
Aspergillus niger
amyloglucosidase
-
Rhizopus arrhizus
amyloglucosidase
-
Aspergillus oryzae
amyloglucosidase
-
Aspergillus terreus
amyloglucosidase
-
Trichoderma reesei
amyloglucosidase
-
Aspergillus awamori
amyloglucosidase
-
Rhizopus niveus
amyloglucosidase
-
Mucor javanicus
amyloglucosidase
-
Aspergillus foetidus
amyloglucosidase
-
Mycothermus thermophilus
amyloglucosidase
-
Mucor rouxians
amyloglucosidase
-
Arthrobotrys amerospora
amyloglucosidase
-
Monascus kaoliang
GA
-
Neurospora crassa
GA
-
Aspergillus niger
GA
-
Rhizopus arrhizus
GA
-
Aspergillus oryzae
GA
-
Aspergillus terreus
GA
-
Aspergillus phoenicis
GA
-
Trichoderma reesei
GA
-
Aspergillus awamori
GA
-
Rhizopus niveus
GA
-
Mucor javanicus
GA
-
Aspergillus foetidus
GA
-
Rhizopus microsporus var. oligosporus
GA
-
Mycothermus thermophilus
GA
-
Mucor rouxians
GA
-
Arthrobotrys amerospora
GA
-
Monascus kaoliang
gamma-amylase
-
Neurospora crassa
gamma-amylase
-
Aspergillus niger
gamma-amylase
-
Rhizopus arrhizus
gamma-amylase
-
Aspergillus oryzae
gamma-amylase
-
Aspergillus terreus
gamma-amylase
-
Trichoderma reesei
gamma-amylase
-
Aspergillus awamori
gamma-amylase
-
Rhizopus niveus
gamma-amylase
-
Mucor javanicus
gamma-amylase
-
Aspergillus foetidus
gamma-amylase
-
Mycothermus thermophilus
gamma-amylase
-
Mucor rouxians
gamma-amylase
-
Arthrobotrys amerospora
gamma-amylase
-
Monascus kaoliang
glucoamylase
-
Neurospora crassa
glucoamylase
-
Aspergillus niger
glucoamylase
-
Rhizopus arrhizus
glucoamylase
-
Aspergillus oryzae
glucoamylase
-
Aspergillus terreus
glucoamylase
-
Aspergillus phoenicis
glucoamylase
-
Trichoderma reesei
glucoamylase
-
Aspergillus awamori
glucoamylase
-
Rhizopus niveus
glucoamylase
-
Mucor javanicus
glucoamylase
-
Aspergillus foetidus
glucoamylase
-
Rhizopus microsporus var. oligosporus
glucoamylase
-
Mycothermus thermophilus
glucoamylase
-
Mucor rouxians
glucoamylase
-
Arthrobotrys amerospora
glucoamylase
-
Monascus kaoliang
glucoamylase C
-
Rhizopus niveus
glucoamylase D
-
Rhizopus niveus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Aspergillus niger
50
-
strain NRRL 330 Aspergillus niger
55
-
-
Arthrobotrys amerospora
60
-
-
Aspergillus awamori
70
-
-
Trichoderma reesei
70
-
-
Mycothermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5 5 several isozymes Aspergillus niger
4.5
-
active form 1 Monascus kaoliang
4.5
-
active enzyme form I Monascus kaoliang
4.7
-
active form 2 Monascus kaoliang
4.7
-
active enzyme form II Monascus kaoliang
5.4
-
mutant strain Neurospora crassa
6
-
-
Arthrobotrys amerospora

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 7 stable Aspergillus terreus
3 7 stable at Aspergillus terreus