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Literature summary extracted from

  • Yang, J.; Li, L.; Xiao, Y.; Li, J.; Long, L.; Wang, F.; Zhang, S.
    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)

EC Number Cloned (Comment) Organism
3.2.1.1 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

EC Number Protein Variants Comment Organism
3.2.1.1 K205L site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209A site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209C site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209D site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209E site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209F site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209G site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209H site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209I site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209L site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209M site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209N site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209P site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209Q site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209R site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209S site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209T site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209V site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209W site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 K209Y site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 Y187E site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme uncultured bacterium
3.2.1.1 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

EC Number Organism UniProt Comment Textmining
3.2.1.1 uncultured bacterium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 soluble starch + H2O
-
 uncultured bacterium ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 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

EC Number Synonyms Comment Organism
3.2.1.1 AMY121
-
 uncultured bacterium
3.2.1.1 endo-1,4-alpha-D-glucan glucohydrolase
-
 uncultured bacterium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 55 80 temperature optima of mutant enzymes, overview uncultured bacterium
3.2.1.1 75
-
 wild-type enzyme uncultured bacterium

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 additional information
-
 addition of hydrophobic interactions and saltbridges can increase the thermostability of variants Y187E and K205L uncultured bacterium
3.2.1.1 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 7.5
-
 assay at uncultured bacterium

General Information

EC Number General Information Comment Organism
3.2.1.1 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