Any feedback?
Literature summary for 3.2.1.1 extracted from
- A chimeric alpha-amylase engineered from Bacillus acidicola and Geobacillus thermoleovorans with improved thermostability and catalytic efficiency (2016), J. Ind. Microbiol. Biotechnol., 43, 473-484 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged chimeric acidic alpha-amylase Ba-Gt-amy in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha | Geobacillus thermoleovorans |
| recombinant expression of His-tagged chimeric acidic alpha-amylase Ba-Gt-amy in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha | Bacillus acidicola |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans | Geobacillus thermoleovorans |
| additional information | construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans | Bacillus acidicola |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ag+ | - |
Bacillus acidicola |  |
| Ag+ | - |
Geobacillus thermoleovorans | |
| Cu2+ | - |
Bacillus acidicola | |
| Cu2+ | - |
Geobacillus thermoleovorans | |
| Hg2+ | strong inhibition | Bacillus acidicola | |
| Hg2+ | strong inhibition | Geobacillus thermoleovorans | |
| Mn2+ | - |
Bacillus acidicola | |
| Mn2+ | - |
Geobacillus thermoleovorans | |
| Ni2+ | - |
Bacillus acidicola | |
| Ni2+ | - |
Geobacillus thermoleovorans | |
| Pb2+ | - |
Bacillus acidicola | |
| Pb2+ | - |
Geobacillus thermoleovorans | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Lineweaver-Burk plot, kinetics and thermodynamics for recombinant chimeric acidic alpha-amylase Ba-Gt-amy, detailed overview. Adsorption kinetics of mutant Ba-Gt-amy and wild-type Ba?amy to 1% raw corn starch. Km and Vmax values of mutant Ba-Gt-amy for soluble starch are 0.8 mg/ml and 10.746 mmol*mg/min, whereas those for wild-type Ba-amy are 1.66 mg/ml and 0.0526 mmol*mg/min, respectively | Bacillus acidicola | |
| additional information | - |
additional information | Lineweaver-Burk plot, kinetics and thermodynamics for recombinant chimeric acidic alpha-amylase Ba-Gt-amy, detailed overview. Adsorption kinetics of mutant Ba-Gt-amy to 1% raw corn starch. Km and Vmax values of mutant Ba-Gt-amy for soluble starch are 0.8 mg/ml and 10.746 mmol * mg/min | Geobacillus thermoleovorans |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates the recombinant chimeric mutant amylase | Geobacillus thermoleovorans | |
| Co2+ | activates the recombinant chimeric mutant amylase | Bacillus acidicola | |
| Mg2+ | activates the recombinant chimeric mutant amylase | Geobacillus thermoleovorans | |
| Mg2+ | activates the recombinant chimeric mutant amylase | Bacillus acidicola | |
| additional information | the recombinant chimeric mutant amylase activity is not significantly affected by EGTA, Ca2+, Na+, and K+. The enzymes are Ca2+-independent | Geobacillus thermoleovorans | |
| additional information | the recombinant chimeric mutant amylase activity is not significantly affected by EGTA, Ca2+, Na+, and K+. The enzymes are Ca2+-independent | Bacillus acidicola |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus acidicola | - |
- |
- |
| Geobacillus thermoleovorans | J9PXA2 | - |
- |
| Geobacillus thermoleovorans MTCC 4220 | J9PXA2 | - |
- |
| Geobacillus thermoleovorans NP-54 | J9PXA2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged chimeric acidic alpha-amylase Ba-Gt-amy from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Geobacillus thermoleovorans |
| recombinant His-tagged chimeric acidic alpha-amylase Ba-Gt-amy from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus acidicola |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| corn starch + H2O | 1% starch solution | Geobacillus thermoleovorans | maltose + maltotriose + maltotetraose | - |
? | |
| corn starch + H2O | 1% starch solution | Bacillus acidicola | maltose + maltotriose + maltotetraose | - |
? | |
| corn starch + H2O | 1% starch solution | Geobacillus thermoleovorans NP-54 | maltose + maltotriose + maltotetraose | - |
? | |
| corn starch + H2O | 1% starch solution | Geobacillus thermoleovorans MTCC 4220 | maltose + maltotriose + maltotetraose | - |
? | |
| additional information | applicability of recombinant chimeric mutant Ba-Gt-amy and wild-type amylase Ba-amy in raw starch hydrolysis, method evaluation | Bacillus acidicola | ? | - |
? | |
| additional information | applicability of recombinant chimeric mutant Ba-Gt-amy in raw starch hydrolysis, method evaluation | Geobacillus thermoleovorans | ? | - |
? | |
| additional information | applicability of recombinant chimeric mutant Ba-Gt-amy in raw starch hydrolysis, method evaluation | Geobacillus thermoleovorans NP-54 | ? | - |
? | |
| additional information | applicability of recombinant chimeric mutant Ba-Gt-amy in raw starch hydrolysis, method evaluation | Geobacillus thermoleovorans MTCC 4220 | ? | - |
? | |
| potato starch + H2O | 0.5% starch solution | Geobacillus thermoleovorans | maltose + maltotriose + maltotetraose | - |
? | |
| potato starch + H2O | 0.5% starch solution | Bacillus acidicola | maltose + maltotriose + maltotetraose | - |
? | |
| potato starch + H2O | 0.5% starch solution | Geobacillus thermoleovorans NP-54 | maltose + maltotriose + maltotetraose | - |
? | |
| potato starch + H2O | 0.5% starch solution | Geobacillus thermoleovorans MTCC 4220 | maltose + maltotriose + maltotetraose | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acidic amylase | - |
Bacillus acidicola |
| Ba-amy | - |
Bacillus acidicola |
| Gt-amy | - |
Geobacillus thermoleovorans |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
recombinant chimeric acidic alpha-amylase Ba-Gt-amy | Geobacillus thermoleovorans |
| 60 | - |
recombinant wild-type Ba-amy enzyme | Bacillus acidicola |
| 60 | 70 | recombinant chimeric mutant Ba-Gt-amy | Bacillus acidicola |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
determination of thermal denaturation kinetics of the recombinant His-tagged chimeric acidic alpha-amylase Ba-Gt-amy, overview | Geobacillus thermoleovorans |
| additional information | - |
determination of thermal denaturation kinetics of the recombinant His-tagged chimeric acidic alpha-amylase Ba-Gt-amy, overview | Bacillus acidicola |
| 70 | - |
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 44 min, of recombinant wild-type Ba-amy 25 min | Bacillus acidicola |
| 70 | - |
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 44 min, of recombinant wild-type Gt-amy 238 min | Geobacillus thermoleovorans |
| 80 | - |
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 30 min | Geobacillus thermoleovorans |
| 80 | - |
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 30 min, of recombinant wild-type Ba-amy 15 min | Bacillus acidicola |
| 90 | - |
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 15 min | Geobacillus thermoleovorans |
| 90 | - |
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 15 min, of recombinant wild-type Ba-amy 5 min | Bacillus acidicola |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 5 | recombinant chimeric acidic alpha-amylase Ba-Gt-amy, assay at | Geobacillus thermoleovorans |
| 4 | 5 | recombinant wild-type Ba-amy enzyme and chimeric mutant Ba-Gt-amy | Bacillus acidicola |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 6 | recombinant chimeric acidic alpha-amylase Ba-Gt-amy, activity range | Geobacillus thermoleovorans |
| 3 | 6 | recombinant chimeric acidic alpha-amylase Ba-Gt-amy, activity range | Bacillus acidicola |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 5 | purified recombinant chimeric acidic alpha-amylase Ba-Gt-amy, 12 h, 90% activity remaining | Geobacillus thermoleovorans |
| 4 | 5 | purified recombinant chimeric acidic alpha-amylase Ba-Gt-amy, 12 h, 90% activity remaining | Bacillus acidicola |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
