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Literature summary extracted from
- Fungal glucoamylases (2005), Biotechnol. Adv., 24, 80-85.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | industry | Rhizopus enzymes are useful in industrial applications | Rhizopus arrhizus |
| 3.2.1.3 | industry | the enzyme is useful in industrial applications | Aspergillus niger |
| 3.2.1.3 | industry | the enzyme is useful in industrial applications | Aspergillus oryzae |
| 3.2.1.3 | industry | the enzyme is useful in industrial applications | Aspergillus phoenicis |
| 3.2.1.3 | industry | the enzyme is useful in industrial applications | Rhizopus niveus |
| 3.2.1.3 | industry | the enzyme is useful in industrial applications | Rhizopus microsporus var. oligosporus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | additional information | improvement of enzyme for inductrial applications | Aspergillus niger |
| 3.2.1.3 | additional information | improvement of enzyme for inductrial applications | Rhizopus arrhizus |
| 3.2.1.3 | additional information | improvement of enzyme for industrial applications | Rhizopus niveus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Neurospora crassa | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Aspergillus niger | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Rhizopus arrhizus | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Aspergillus oryzae | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Aspergillus terreus | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Trichoderma reesei | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Aspergillus awamori | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Rhizopus niveus | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Mucor javanicus | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Aspergillus foetidus | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Mycothermus thermophilus | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Mucor rouxians | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Arthrobotrys amerospora | 5618 | - |
| 3.2.1.3 | cell wall | the enzyme is adsorbed to the cell wall | Monascus kaoliang | 5618 | - |
| 3.2.1.3 | extracellular | - |
Neurospora crassa | - |
- |
| 3.2.1.3 | extracellular | - |
Aspergillus niger | - |
- |
| 3.2.1.3 | extracellular | - |
Rhizopus arrhizus | - |
- |
| 3.2.1.3 | extracellular | - |
Aspergillus oryzae | - |
- |
| 3.2.1.3 | extracellular | - |
Aspergillus terreus | - |
- |
| 3.2.1.3 | extracellular | - |
Aspergillus phoenicis | - |
- |
| 3.2.1.3 | extracellular | - |
Trichoderma reesei | - |
- |
| 3.2.1.3 | extracellular | - |
Aspergillus awamori | - |
- |
| 3.2.1.3 | extracellular | - |
Rhizopus niveus | - |
- |
| 3.2.1.3 | extracellular | - |
Mucor javanicus | - |
- |
| 3.2.1.3 | extracellular | - |
Aspergillus foetidus | - |
- |
| 3.2.1.3 | extracellular | - |
Rhizopus microsporus var. oligosporus | - |
- |
| 3.2.1.3 | extracellular | - |
Mycothermus thermophilus | - |
- |
| 3.2.1.3 | extracellular | - |
Mucor rouxians | - |
- |
| 3.2.1.3 | extracellular | - |
Arthrobotrys amerospora | - |
- |
| 3.2.1.3 | extracellular | - |
Monascus kaoliang | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 125000 | - |
- |
Aspergillus niger |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | 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 + ? | - |
? |  |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | starch + H2O | Neurospora crassa | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus niger | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Rhizopus arrhizus | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus oryzae | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus terreus | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus phoenicis | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Trichoderma reesei | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus awamori | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Rhizopus niveus | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Mucor javanicus | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus foetidus | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Rhizopus microsporus var. oligosporus | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Mycothermus thermophilus | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Mucor rouxians | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Arthrobotrys amerospora | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | Monascus kaoliang | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | starch + H2O | Monascus kaoliang F-1 | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus awamori X-100 | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus terreus NA-170 | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus niger NRRL 330 | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus terreus NA-770 | the enzyme is required for degradation of raw starch | starch + beta-D-glucose | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.3 | Arthrobotrys amerospora | - |
- |
- |
| 3.2.1.3 | Aspergillus awamori | - |
- |
- |
| 3.2.1.3 | Aspergillus awamori | - |
var. kawachi | - |
| 3.2.1.3 | Aspergillus awamori X-100 | - |
- |
- |
| 3.2.1.3 | Aspergillus foetidus | - |
- |
- |
| 3.2.1.3 | Aspergillus niger | - |
- |
- |
| 3.2.1.3 | Aspergillus niger | - |
at least six isozymes, several strains, e.g. strain NRRL 330 | - |
| 3.2.1.3 | Aspergillus niger NRRL 330 | - |
- |
- |
| 3.2.1.3 | Aspergillus oryzae | - |
- |
- |
| 3.2.1.3 | Aspergillus phoenicis | - |
- |
- |
| 3.2.1.3 | Aspergillus terreus | - |
- |
- |
| 3.2.1.3 | Aspergillus terreus NA-170 | - |
- |
- |
| 3.2.1.3 | Aspergillus terreus NA-770 | - |
- |
- |
| 3.2.1.3 | Monascus kaoliang | - |
two active forms | - |
| 3.2.1.3 | Monascus kaoliang | - |
nov-sp. F-1 | - |
| 3.2.1.3 | Monascus kaoliang F-1 | - |
two active forms | - |
| 3.2.1.3 | Mucor javanicus | - |
- |
- |
| 3.2.1.3 | Mucor rouxians | - |
- |
- |
| 3.2.1.3 | Mycothermus thermophilus | - |
- |
- |
| 3.2.1.3 | Neurospora crassa | - |
- |
- |
| 3.2.1.3 | Rhizopus arrhizus | - |
- |
- |
| 3.2.1.3 | Rhizopus microsporus var. oligosporus | - |
- |
- |
| 3.2.1.3 | Rhizopus niveus | - |
- |
- |
| 3.2.1.3 | Rhizopus niveus | - |
isozymes glucoamylase C and D | - |
| 3.2.1.3 | Trichoderma reesei | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | glycoprotein | - |
Aspergillus niger |
| 3.2.1.3 | glycoprotein | - |
Rhizopus arrhizus |
| 3.2.1.3 | glycoprotein | - |
Aspergillus oryzae |
| 3.2.1.3 | glycoprotein | - |
Aspergillus terreus |
| 3.2.1.3 | glycoprotein | - |
Trichoderma reesei |
| 3.2.1.3 | glycoprotein | - |
Aspergillus awamori |
| 3.2.1.3 | glycoprotein | - |
Mucor javanicus |
| 3.2.1.3 | glycoprotein | - |
Aspergillus foetidus |
| 3.2.1.3 | glycoprotein | - |
Mycothermus thermophilus |
| 3.2.1.3 | glycoprotein | - |
Mucor rouxians |
| 3.2.1.3 | glycoprotein | - |
Arthrobotrys amerospora |
| 3.2.1.3 | glycoprotein | - |
Monascus kaoliang |
| 3.2.1.3 | glycoprotein | O-glycosylation | Rhizopus arrhizus |
| 3.2.1.3 | glycoprotein | O-glycosylation | Aspergillus oryzae |
| 3.2.1.3 | glycoprotein | O-glycosylation | Aspergillus terreus |
| 3.2.1.3 | glycoprotein | O-glycosylation | Aspergillus phoenicis |
| 3.2.1.3 | glycoprotein | O-glycosylation | Trichoderma reesei |
| 3.2.1.3 | glycoprotein | O-glycosylation | Mucor javanicus |
| 3.2.1.3 | glycoprotein | O-glycosylation | Aspergillus foetidus |
| 3.2.1.3 | glycoprotein | O-glycosylation | Rhizopus microsporus var. oligosporus |
| 3.2.1.3 | glycoprotein | O-glycosylation | Mycothermus thermophilus |
| 3.2.1.3 | glycoprotein | O-glycosylation | Mucor rouxians |
| 3.2.1.3 | glycoprotein | O-glycosylation | Arthrobotrys amerospora |
| 3.2.1.3 | glycoprotein | O-glycosylation | Monascus kaoliang |
| 3.2.1.3 | glycoprotein | deglycosylation of the enzyme leads to reduced thermal stability and a decrease in enzyme secretion, O-glycosylation | Aspergillus awamori |
| 3.2.1.3 | glycoprotein | O-glycosylation, 5.1% carbohydrate content | Neurospora crassa |
| 3.2.1.3 | glycoprotein | O-glycosylation, isozymes glucoamylase C and D have 14.9% and 12.7% carbohydrate content, respectively | Rhizopus niveus |
| 3.2.1.3 | glycoprotein | O-glycosylation, required for enzyme stability and activity, structure overview | Aspergillus niger |
| 3.2.1.3 | glycoprotein | glucoamylase C and D contain 14.9% and 12.7% carbohydrate, respectively | Rhizopus niveus |
| 3.2.1.3 | glycoprotein | the enzyme contains 5.1% carbohydrate | Neurospora crassa |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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 | |
| 3.2.1.3 | (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
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.2.1.3 | additional information | culture conditions for enzyme production, overview | Aspergillus niger | - |
| 3.2.1.3 | additional information | culture conditions for enzyme production, overview | Rhizopus arrhizus | - |
| 3.2.1.3 | additional information | culture conditions for enzyme production, overview | Rhizopus niveus | - |
| 3.2.1.3 | additional information | culture conditions for enzyme production, overview | Rhizopus microsporus var. oligosporus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | 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 + ? | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Neurospora crassa | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Rhizopus arrhizus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Aspergillus terreus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Trichoderma reesei | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Aspergillus awamori | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Rhizopus niveus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Mucor javanicus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Aspergillus foetidus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Rhizopus microsporus var. oligosporus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Mycothermus thermophilus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Mucor rouxians | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Monascus kaoliang | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Neurospora crassa | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus niger | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Rhizopus arrhizus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus oryzae | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus terreus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus phoenicis | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Trichoderma reesei | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus awamori | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Rhizopus niveus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Mucor javanicus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus foetidus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Rhizopus microsporus var. oligosporus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Mycothermus thermophilus | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Mucor rouxians | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Arthrobotrys amerospora | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Monascus kaoliang | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme contains 7 subsites for substrate binding, subsite affinities | Aspergillus niger | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme contains 7 subsites for substrate binding, subsite affinities | Aspergillus oryzae | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme contains 7 subsites for substrate binding, subsite affinities | Aspergillus phoenicis | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme contains 7 subsites for substrate binding, subsite affinities | Arthrobotrys amerospora | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Monascus kaoliang F-1 | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Monascus kaoliang F-1 | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Aspergillus awamori X-100 | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus awamori X-100 | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Aspergillus terreus NA-170 | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus terreus NA-170 | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus niger NRRL 330 | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme contains 7 subsites for substrate binding, subsite affinities | Aspergillus niger NRRL 330 | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Aspergillus terreus NA-770 | starch + beta-D-glucose | - |
? | |
| 3.2.1.3 | starch + H2O | the enzyme is required for degradation of raw starch | Aspergillus terreus NA-770 | starch + beta-D-glucose | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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 |
| 3.2.1.3 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | amyloglucosidase | - |
Neurospora crassa |
| 3.2.1.3 | amyloglucosidase | - |
Aspergillus niger |
| 3.2.1.3 | amyloglucosidase | - |
Rhizopus arrhizus |
| 3.2.1.3 | amyloglucosidase | - |
Aspergillus oryzae |
| 3.2.1.3 | amyloglucosidase | - |
Aspergillus terreus |
| 3.2.1.3 | amyloglucosidase | - |
Trichoderma reesei |
| 3.2.1.3 | amyloglucosidase | - |
Aspergillus awamori |
| 3.2.1.3 | amyloglucosidase | - |
Rhizopus niveus |
| 3.2.1.3 | amyloglucosidase | - |
Mucor javanicus |
| 3.2.1.3 | amyloglucosidase | - |
Aspergillus foetidus |
| 3.2.1.3 | amyloglucosidase | - |
Mycothermus thermophilus |
| 3.2.1.3 | amyloglucosidase | - |
Mucor rouxians |
| 3.2.1.3 | amyloglucosidase | - |
Arthrobotrys amerospora |
| 3.2.1.3 | amyloglucosidase | - |
Monascus kaoliang |
| 3.2.1.3 | GA | - |
Neurospora crassa |
| 3.2.1.3 | GA | - |
Aspergillus niger |
| 3.2.1.3 | GA | - |
Rhizopus arrhizus |
| 3.2.1.3 | GA | - |
Aspergillus oryzae |
| 3.2.1.3 | GA | - |
Aspergillus terreus |
| 3.2.1.3 | GA | - |
Aspergillus phoenicis |
| 3.2.1.3 | GA | - |
Trichoderma reesei |
| 3.2.1.3 | GA | - |
Aspergillus awamori |
| 3.2.1.3 | GA | - |
Rhizopus niveus |
| 3.2.1.3 | GA | - |
Mucor javanicus |
| 3.2.1.3 | GA | - |
Aspergillus foetidus |
| 3.2.1.3 | GA | - |
Rhizopus microsporus var. oligosporus |
| 3.2.1.3 | GA | - |
Mycothermus thermophilus |
| 3.2.1.3 | GA | - |
Mucor rouxians |
| 3.2.1.3 | GA | - |
Arthrobotrys amerospora |
| 3.2.1.3 | GA | - |
Monascus kaoliang |
| 3.2.1.3 | gamma-amylase | - |
Neurospora crassa |
| 3.2.1.3 | gamma-amylase | - |
Aspergillus niger |
| 3.2.1.3 | gamma-amylase | - |
Rhizopus arrhizus |
| 3.2.1.3 | gamma-amylase | - |
Aspergillus oryzae |
| 3.2.1.3 | gamma-amylase | - |
Aspergillus terreus |
| 3.2.1.3 | gamma-amylase | - |
Trichoderma reesei |
| 3.2.1.3 | gamma-amylase | - |
Aspergillus awamori |
| 3.2.1.3 | gamma-amylase | - |
Rhizopus niveus |
| 3.2.1.3 | gamma-amylase | - |
Mucor javanicus |
| 3.2.1.3 | gamma-amylase | - |
Aspergillus foetidus |
| 3.2.1.3 | gamma-amylase | - |
Mycothermus thermophilus |
| 3.2.1.3 | gamma-amylase | - |
Mucor rouxians |
| 3.2.1.3 | gamma-amylase | - |
Arthrobotrys amerospora |
| 3.2.1.3 | gamma-amylase | - |
Monascus kaoliang |
| 3.2.1.3 | glucoamylase | - |
Neurospora crassa |
| 3.2.1.3 | glucoamylase | - |
Aspergillus niger |
| 3.2.1.3 | glucoamylase | - |
Rhizopus arrhizus |
| 3.2.1.3 | glucoamylase | - |
Aspergillus oryzae |
| 3.2.1.3 | glucoamylase | - |
Aspergillus terreus |
| 3.2.1.3 | glucoamylase | - |
Aspergillus phoenicis |
| 3.2.1.3 | glucoamylase | - |
Trichoderma reesei |
| 3.2.1.3 | glucoamylase | - |
Aspergillus awamori |
| 3.2.1.3 | glucoamylase | - |
Rhizopus niveus |
| 3.2.1.3 | glucoamylase | - |
Mucor javanicus |
| 3.2.1.3 | glucoamylase | - |
Aspergillus foetidus |
| 3.2.1.3 | glucoamylase | - |
Rhizopus microsporus var. oligosporus |
| 3.2.1.3 | glucoamylase | - |
Mycothermus thermophilus |
| 3.2.1.3 | glucoamylase | - |
Mucor rouxians |
| 3.2.1.3 | glucoamylase | - |
Arthrobotrys amerospora |
| 3.2.1.3 | glucoamylase | - |
Monascus kaoliang |
| 3.2.1.3 | glucoamylase C | - |
Rhizopus niveus |
| 3.2.1.3 | glucoamylase D | - |
Rhizopus niveus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 50 | - |
- |
Aspergillus niger |
| 3.2.1.3 | 50 | - |
strain NRRL 330 | Aspergillus niger |
| 3.2.1.3 | 55 | - |
- |
Arthrobotrys amerospora |
| 3.2.1.3 | 60 | - |
- |
Aspergillus awamori |
| 3.2.1.3 | 70 | - |
- |
Trichoderma reesei |
| 3.2.1.3 | 70 | - |
- |
Mycothermus thermophilus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 3.5 | 5 | several isozymes | Aspergillus niger |
| 3.2.1.3 | 4.5 | - |
active form 1 | Monascus kaoliang |
| 3.2.1.3 | 4.5 | - |
active enzyme form I | Monascus kaoliang |
| 3.2.1.3 | 4.7 | - |
active form 2 | Monascus kaoliang |
| 3.2.1.3 | 4.7 | - |
active enzyme form II | Monascus kaoliang |
| 3.2.1.3 | 5.4 | - |
mutant strain | Neurospora crassa |
| 3.2.1.3 | 6 | - |
- |
Arthrobotrys amerospora |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 3 | 7 | stable | Aspergillus terreus |
| 3.2.1.3 | 3 | 7 | stable at | Aspergillus terreus |
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Release 2023.1 (January 2023)
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