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Literature summary for 5.4.99.39 extracted from
- beta-Amyrin synthase, one of the most important key enzymes for triterpene skeleton formation in higher plants (2018), Pak. J. Bot., 50, 231-243 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene beta-AS, sequence comparisons and phylogenetic analysis | Euphorbia tirucalli |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Glycine max |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Glycyrrhiza uralensis |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Avena longiglumis |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Artemisia annua |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Bupleurum chinense |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Panax quinquefolius |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Panax japonicus |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Gypsophila vaccaria |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Barbarea vulgaris |
| gene beta-AS, sequence comparisons and phylogenetic analysis | Polygala tenuifolia |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | beta-AS of Avena longiglumis is anchored to a specific site in the cytoplasmic matrix to perform the catalytic function | Avena longiglumis | 5737 | - |
| additional information | beta-AS of Panax japonicus does not cross the membrane | Panax japonicus | - |
- |
| additional information | beta-AS of Panax quinquefolius does not cross the membrane | Panax quinquefolius | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Medicago truncatula | - |
beta-amyrin | - |
r |  |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Euphorbia tirucalli | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Glycine max | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Glycyrrhiza uralensis | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Avena longiglumis | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Artemisia annua | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Bupleurum chinense | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Panax quinquefolius | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Panax japonicus | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Gypsophila vaccaria | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Barbarea vulgaris | - |
beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | Polygala tenuifolia | - |
beta-amyrin | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Artemisia annua | B1P7H3 | - |
- |
| Avena longiglumis | Q6IWA0 | - |
- |
| Barbarea vulgaris | H9NAL5 | - |
- |
| Bupleurum chinense | B0ZSP3 | - |
- |
| Euphorbia tirucalli | Q401R6 | - |
- |
| Glycine max | Q8H2B0 | - |
- |
| Glycyrrhiza uralensis | D7P7W7 | - |
- |
| Gypsophila vaccaria | A3E7Y8 | - |
- |
| Medicago truncatula | - |
- |
- |
| Panax japonicus | A0A0H3YJP6 | - |
- |
| Panax quinquefolius | N0BQ25 | - |
- |
| Polygala tenuifolia | A1E4D1 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell suspension culture | - |
Medicago truncatula | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Euphorbia tirucalli | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Glycine max | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Glycyrrhiza uralensis | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Avena longiglumis | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Artemisia annua | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Bupleurum chinense | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Panax quinquefolius | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Panax japonicus | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Gypsophila vaccaria | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Barbarea vulgaris | - |
| additional information | analysis of temporal and spatial specificity of the expression of beta-AS | Polygala tenuifolia | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Medicago truncatula | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Euphorbia tirucalli | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Glycine max | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Glycyrrhiza uralensis | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Avena longiglumis | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Artemisia annua | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Bupleurum chinense | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Panax quinquefolius | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Panax japonicus | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Gypsophila vaccaria | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Barbarea vulgaris | beta-amyrin | - |
r | |
| (3S)-2,3-epoxy-2,3-dihydrosqualene | - |
Polygala tenuifolia | beta-amyrin | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 84604, sequence calculation | Glycine max |
| ? | x * 86859, sequence calculation | Avena longiglumis |
| ? | x * 87073, sequence calculation | Glycyrrhiza uralensis |
| ? | x * 87343, sequence calculation | Polygala tenuifolia |
| ? | x * 87503, sequence calculation | Artemisia annua |
| ? | x * 87503, sequence calculation | Barbarea vulgaris |
| ? | x * 87521, sequence calculation | Gypsophila vaccaria |
| ? | x * 87590, sequence calculation | Euphorbia tirucalli |
| ? | x * 87775, sequence calculation | Panax quinquefolius |
| ? | x * 87791, sequence calculation | Bupleurum chinense |
| ? | x * 87900, sequence calculation | Panax japonicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AMS1 | - |
Glycine max |
| BAS2 | - |
Panax quinquefolius |
| beta-AS | - |
Medicago truncatula |
| beta-AS | - |
Euphorbia tirucalli |
| beta-AS | - |
Glycine max |
| beta-AS | - |
Glycyrrhiza uralensis |
| beta-AS | - |
Avena longiglumis |
| beta-AS | - |
Artemisia annua |
| beta-AS | - |
Bupleurum chinense |
| beta-AS | - |
Panax quinquefolius |
| beta-AS | - |
Panax japonicus |
| beta-AS | - |
Gypsophila vaccaria |
| beta-AS | - |
Barbarea vulgaris |
| beta-AS | - |
Polygala tenuifolia |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Panax japonicus | sequence calculation | - |
5.84 |
| Artemisia annua | sequence calculation | - |
5.87 |
| Gypsophila vaccaria | sequence calculation | - |
5.89 |
| Panax quinquefolius | sequence calculation | - |
5.92 |
| Bupleurum chinense | sequence calculation | - |
6.02 |
| Glycine max | sequence calculation | - |
6.1 |
| Avena longiglumis | sequence calculation | - |
6.12 |
| Glycyrrhiza uralensis | sequence calculation | - |
6.19 |
| Polygala tenuifolia | sequence calculation | - |
6.21 |
| Barbarea vulgaris | sequence calculation | - |
6.29 |
| Euphorbia tirucalli | sequence calculation | - |
6.78 |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Medicago truncatula | the enzyme is inducible by methyl jasmonate by 50fold in cell suspension cultures | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Medicago truncatula |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Euphorbia tirucalli |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Glycine max |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Glycyrrhiza uralensis |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Avena longiglumis |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Artemisia annua |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Bupleurum chinense |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Panax quinquefolius |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Panax japonicus |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Gypsophila vaccaria |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Barbarea vulgaris |
| evolution | analysis of conserved domains and the evolutionary relationships between different beta-amyrin synthases from plants, sequence comparisons and phylogenetic analysis, detailed overview. The enzyme belongs to the family of oxidosqualene cyclases (OSC) | Polygala tenuifolia |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Medicago truncatula |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Euphorbia tirucalli |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Glycine max |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Glycyrrhiza uralensis |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Avena longiglumis |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Artemisia annua |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Bupleurum chinense |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Panax quinquefolius |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Panax japonicus |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Gypsophila vaccaria |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Barbarea vulgaris |
| metabolism | beta-amyrin synthase (beta-AS) is an important key enzyme in the mevalonic acid (MVA) pathway. It is a cyclase responsible for cyclization of 2,3-oxidosqualene into beta-amyrin, which is defined as an important branch point between primary and secondary metabolism. beta-AS is responsible for the production of oleanane-type triterpene saponin | Polygala tenuifolia |
| additional information | beta-AS of Panax japonicus does not cross the membrane, three-dimensional enzyme structure modeling | Panax japonicus |
| additional information | beta-AS of Panax quinquefolius does not cross the membrane, three-dimensional enzyme structure modeling | Panax quinquefolius |
| additional information | three-dimensional enzyme structure modeling | Avena longiglumis |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Medicago truncatula |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Euphorbia tirucalli |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Glycine max |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Glycyrrhiza uralensis |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Avena longiglumis |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Artemisia annua |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Bupleurum chinense |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Panax quinquefolius |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Panax japonicus |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Gypsophila vaccaria |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Barbarea vulgaris |
| physiological function | beta-amyrin synthase is one of the most important key enzymes for triterpene skeleton formation in higher plants | Polygala tenuifolia |
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