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Literature summary extracted from
- Heterologous expression of a hyperthermophilic alpha-amylase in xanthan gum producing Xanthomonas campestris cells (2008), Appl. Biochem. Biotechnol., 149, 99-108.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.1 | transfer and heterologous expression of the gene in Xanthomonas campestris ATCC 13951. The transformed Xanthomonas produces similar levels of recombinant alpha-amylase activity, regardless of the carbon source present in growth medium, whereas the native Xanthomonas alpha-amylase production is highly dependent on starch availability and it is supressed in the presence of glucosse or other reducing sugars | Pyrococcus woesei |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.1 | extracellular | native alpha-amylase | Pyrococcus woesei | - |
- |
| 3.2.1.1 | intracellular | recombinant protein in Xanthomonas campestris, a Gram-negative bacterium | Pyrococcus woesei | 5622 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.1 | additional information | Xanthomonas campestris | alpha-Amylase production is highly dependent on starch availability and is supressed in the presence of glucose or other reducing sugars whereas the transformed Xanthomonas expressing the hyperthermophilic alpha-amylase from Pyrococcus woesei produces similar levels of recombinant alpha-amylase activity, regardless of the carbon source present in growth medium | ? | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | Pyrococcus woesei | - |
a hyperthermophilic organism | - |
| 3.2.1.1 | Xanthomonas campestris | - |
a Gram-negative bacterium. alpha-Amylase production is highly dependent on starch availability and is supressed in the presence of glucose or other reducing sugars whereas the transformed Xanthomonas expressing the hyperthermophilic alpha-amylase from Pyrococcus woesei produces similar levels of recombinant alpha-amylase activity, regardless of the carbon source present in growth medium | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.1 | additional information | alpha-Amylase production is highly dependent on starch availability and is supressed in the presence of glucose or other reducing sugars whereas the transformed Xanthomonas expressing the hyperthermophilic alpha-amylase from Pyrococcus woesei produces similar levels of recombinant alpha-amylase activity, regardless of the carbon source present in growth medium | Xanthomonas campestris | ? | - |
? | |
| 3.2.1.1 | starch + H2O | - |
Pyrococcus woesei | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | hyperthermophilic alpha-amylase | classified in family 13 of the glucosyl hydrolase superfamily | Pyrococcus woesei |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 37 | - |
assay at | Xanthomonas campestris |
| 3.2.1.1 | 60 | - |
optimum of the native protein, lower thermophilicity than recombinant protein. The hyperthermophilic alpha-amylase gene from Pyrococcus woesei heterologously expressed in Xanthomonas campestris shows optimal acivity at 95-100°C | Xanthomonas campestris |
| 3.2.1.1 | 95 | - |
assay at, recombinant protein | Pyrococcus woesei |
| 3.2.1.1 | 95 | 100 | recombinant protein | Pyrococcus woesei |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 20 | 145 | 47% relative activity at 20°C, 37% relative activity at 145°C. The natural enzyme displays a steep rise of activity while it declines sharply above 80°C | Xanthomonas campestris |
| 3.2.1.1 | 60 | 145 | recombinant protein, 26% relative activity at 60°C, 50% relative activity at 145°C | Pyrococcus woesei |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 40 | - |
half-life after 4 h incubation | Xanthomonas campestris |
| 3.2.1.1 | 50 | - |
half-life after 2 h incubation | Xanthomonas campestris |
| 3.2.1.1 | 70 | - |
more than 60% of the activity is lost within the first 30 min | Xanthomonas campestris |
| 3.2.1.1 | 90 | - |
stable for 4 h, recombinant protein in Xanthomonas campestris shows similar thermostability as the native Pyrococcus woesei enzyme | Pyrococcus woesei |
| 3.2.1.1 | 100 | - |
85% of its initial activity after 4 h incubation, recombinant protein in Xanthomonas campestris | Pyrococcus woesei |
| 3.2.1.1 | 110 | - |
more than 50% of its initial activity after 4 h incubation, recombinant protein in Xanthomonas campestris | Pyrococcus woesei |
| 3.2.1.1 | 120 | - |
more than 50% of its initial activity after 0.75 h incubation, recombinant protein in Xanthomonas campestris | Pyrococcus woesei |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 5.5 | - |
assay at | Xanthomonas campestris |
| 3.2.1.1 | 5.5 | - |
assay at, recombinant protein | Pyrococcus woesei |
| 3.2.1.1 | 5.5 | 6 | optimum of the recombinant protein | Pyrococcus woesei |
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Release 2023.1 (January 2023)
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