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Literature summary extracted from
- Purification studies on a thermo-active amidase of Geobacillus pallidus BTP-5x MTCC 9225 isolated from thermal springs of Tatapani (Himachal Pradesh) (2013), Appl. Biochem. Biotechnol., 169, 1-14.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.4 | 8-hydroxyquinoline | 18% activation aat 1 mM | Aeribacillus pallidus |  |
| 3.5.1.4 | hydroxylamine | 11% activation aat 1 mM | Aeribacillus pallidus | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.1.4 | DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain DH5alpha, sequence comparison | Aeribacillus pallidus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.4 | 2-mercaptoethanol | 9% inhibition at 1 mM | Aeribacillus pallidus | |
| 3.5.1.4 | Ag+ | complete inhibition at 1 mM | Aeribacillus pallidus | |
| 3.5.1.4 | Cd2+ | 98% inhibition at 1 mM | Aeribacillus pallidus | |
| 3.5.1.4 | Co2+ | 52% inhibition at 1 mM | Aeribacillus pallidus | |
| 3.5.1.4 | Cu2+ | complete inhibition at 1 mM | Aeribacillus pallidus | |
| 3.5.1.4 | Hg2+ | complete inhibition at 1 mM | Aeribacillus pallidus | |
| 3.5.1.4 | L-ascorbic acid | 19% inhibition at 1 mM | Aeribacillus pallidus | |
| 3.5.1.4 | additional information | the enzyme shows resistance to metal chelating agents EDTA, 8-hydroxyquinoline, and sodium azide and is not inhibited by DTT and PMSF or by ammonium persulfate | Aeribacillus pallidus | |
| 3.5.1.4 | phenyl hydrazine | complete inhibition at 1 mM | Aeribacillus pallidus | |
| 3.5.1.4 | Urea | 47% inhibition at 1 mM | Aeribacillus pallidus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.4 | 10.54 | - |
Acrylamide | pH 8.0, 50°C | Aeribacillus pallidus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.4 | additional information | no metalloenzyme, no effect on enzyme activity by Fe2+, Mn2+, Mg2+, and Ca2+ | Aeribacillus pallidus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.4 | 38400 | - |
4 * 38500, SDS-PAGE, 4 * 38400, about, sequence calculation | Aeribacillus pallidus |
| 3.5.1.4 | 38500 | - |
4 * 38500, SDS-PAGE, 4 * 38400, about, sequence calculation | Aeribacillus pallidus |
| 3.5.1.4 | 158000 | - |
native PAGE | Aeribacillus pallidus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.4 | Aeribacillus pallidus | - |
isolated from thermal springs of Tatapani (Himachal Pradesh) | - |
| 3.5.1.4 | Aeribacillus pallidus BTP-5x MTCC 9225 | - |
isolated from thermal springs of Tatapani (Himachal Pradesh) | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.1.4 | native enzyme 6.2fold to apparent homogeneity by anion exchange chromatography and gel filtration | Aeribacillus pallidus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.4 | 30.49 | - |
purified native enzyme, pH 8.0, 50°C | Aeribacillus pallidus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.4 | acetamide + H2O | high activity | Aeribacillus pallidus | acetate + NH3 | - |
? | |
| 3.5.1.4 | acetamide + H2O | high activity | Aeribacillus pallidus BTP-5x MTCC 9225 | acetate + NH3 | - |
? | |
| 3.5.1.4 | acrylamide + H2O | - |
Aeribacillus pallidus | acrylate + NH3 | - |
? | |
| 3.5.1.4 | acrylamide + H2O | - |
Aeribacillus pallidus BTP-5x MTCC 9225 | acrylate + NH3 | - |
? | |
| 3.5.1.4 | formamide + H2O | - |
Aeribacillus pallidus | formate + NH3 | - |
? | |
| 3.5.1.4 | formamide + H2O | - |
Aeribacillus pallidus BTP-5x MTCC 9225 | formate + NH3 | - |
? | |
| 3.5.1.4 | lactamide + H2O | - |
Aeribacillus pallidus | lactate + NH3 | - |
? | |
| 3.5.1.4 | additional information | the enzyme preferentially hydrolyzes small aliphatic amides and has a narrow substrate spectrum, overview. Poor activity with methacrylamide, N-methyl acetamide, cyanoacetamide, and butyramide. No activity with thioacetamide, trimethylacetamide, N-ethylacetamide, dimethylformamide, nicotinamide, and benzamide | Aeribacillus pallidus | ? | - |
? | |
| 3.5.1.4 | additional information | the enzyme preferentially hydrolyzes small aliphatic amides and has a narrow substrate spectrum, overview. Poor activity with methacrylamide, N-methyl acetamide, cyanoacetamide, and butyramide. No activity with thioacetamide, trimethylacetamide, N-ethylacetamide, dimethylformamide, nicotinamide, and benzamide | Aeribacillus pallidus BTP-5x MTCC 9225 | ? | - |
? | |
| 3.5.1.4 | propionamide + H2O | best substrate | Aeribacillus pallidus | propionate + NH3 | - |
? | |
| 3.5.1.4 | propionamide + H2O | best substrate | Aeribacillus pallidus BTP-5x MTCC 9225 | propionate + NH3 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.1.4 | homotetramer | 4 * 38500, SDS-PAGE, 4 * 38400, about, sequence calculation | Aeribacillus pallidus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.4 | 60 | - |
broad optimum of 45-70°C | Aeribacillus pallidus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.4 | 30 | 70 | activity range | Aeribacillus pallidus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.4 | additional information | - |
the multimeric nature of the holozyme as a tetramer contributes to protection of the enzyme against thermal denaturation | Aeribacillus pallidus |
| 3.5.1.4 | 50 | 55 | purified enzyme, stable up to 6 h at 50°C, with a t1/2 of 7 h at 55°C | Aeribacillus pallidus |
| 3.5.1.4 | 60 | - |
purified enzyme, pH 8.0, the activity decreases rapidly after 4 h | Aeribacillus pallidus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.4 | 0.0715 | - |
Acrylamide | pH 8.0, 50°C | Aeribacillus pallidus | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.4 | 8.2 | 8.3 | broad optimum of pH 6.0-9.0 | Aeribacillus pallidus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.4 | 4 | 10.5 | activity range | Aeribacillus pallidus |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.5.1.4 | Aeribacillus pallidus | sequence calculation | - |
5.38 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.5.1.4 | additional information | acysteine residue is involved in catalysis | Aeribacillus pallidus |
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