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Literature summary for 3.2.1.1 extracted from
- Identification and thermoadaptation engineering of thermostability conferring residue of deep sea bacterial alpha-amylase AMY121 (2016), J. Mol. Catal. B, 126, 56-63 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloning in Escherichia coli strain XL1-Blue and recombinant expression of His-tagged wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3) | uncultured bacterium |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K205L | site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209A | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209C | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209D | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209E | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209F | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209G | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209H | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209I | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209L | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209M | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209N | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209P | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209Q | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209R | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209S | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209T | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209V | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209W | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| K209Y | site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme | uncultured bacterium |
| Y187E | site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme | uncultured bacterium |
| Y187E/K205L | site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme | uncultured bacterium |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| uncultured bacterium | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, to homogeneity | uncultured bacterium |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| soluble starch + H2O | - |
uncultured bacterium | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the overall structure of amylase AMY121 is composed by three distinct domains (A-C), which are typical in liquefying-type bacterial alpha-amylases, overview | uncultured bacterium |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AMY121 | - |
uncultured bacterium |
| endo-1,4-alpha-D-glucan glucohydrolase | - |
uncultured bacterium |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | 80 | temperature optima of mutant enzymes, overview | uncultured bacterium |
| 75 | - |
wild-type enzyme | uncultured bacterium |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
addition of hydrophobic interactions and saltbridges can increase the thermostability of variants Y187E and K205L | uncultured bacterium |
| 75 | - |
t1/2 values of wild-type AMY121, mutant Y187E, mutant K205L, and mutant Y187E/K205L are 7.04, 7.29, 31.08, and 26.16 min, respectively | uncultured bacterium |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | uncultured bacterium |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | enzyme structure homology model building and structure analysis using analysis multiple sequence alignment, overview. The overall structure of amylase AMY121 is composed by three distinct domains (A-C), which are typical in liquefying-type bacterial alpha-amylases, location of residue Lys209 in domain B | uncultured bacterium |
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