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Literature summary for 2.6.1.B16 extracted from
- Characterization of a novel thermostable (S)-amine-transaminase from an Antarctic moderately-thermophilic bacterium Albidovulum sp. SLM16 (2019), Enzyme Microb. Technol., 131, 109423 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ata_slm16, Phylogenetic analysis, functional recombinant overexpression in Escherichia coli strain BL21 (C2530) | Albidovulum sp. |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics, kinetic parameters 50°C and 65°C, using a pseudo-one substrate kinetic model for ping-pong reaction mechanisms | Albidovulum sp. | |
| 4.4 | - |
(S)-alpha-methylbenzylamine | recombinant enzyme, pH 9.5, 65°C | Albidovulum sp. |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 75000 | - |
recombinant enzyme, gel filtration | Albidovulum sp. |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-alpha-methylbenzylamine + pyruvate | Albidovulum sp. | - |
acetophenone + L-alanine | - |
r | |
| (S)-alpha-methylbenzylamine + pyruvate | Albidovulum sp. SLM16 | - |
acetophenone + L-alanine | - |
r | |
| pyruvate + (S)-1-phenylethylamine | Albidovulum sp. | - |
L-alanine + acetophenone | - |
? | |
| pyruvate + (S)-1-phenylethylamine | Albidovulum sp. SLM16 | - |
L-alanine + acetophenone | - |
? | |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| additional information | the recombinant enzyme shows good stability in the presence of organic solvents | Albidovulum sp. |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Albidovulum sp. | - |
isolated from a geothermal Antarctic environmental sample from a shoreline fumarole in Deception Island | - |
| Albidovulum sp. SLM16 | - |
isolated from a geothermal Antarctic environmental sample from a shoreline fumarole in Deception Island | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli strain BL21(C2530) by centrifugation at 30000 x g for 10 min, heat treatment at 70°C for 10 min, ultrafiltration, and gel filtration | Albidovulum sp. |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| pyruvate + (S)-1-phenylethylamine = L-alanine + acetophenone | ping-pong reaction mechanism | Albidovulum sp. |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 6 | - |
purified recombinant enzyme, pH 9.0, 50°C, substrate (S)-alpha-methylbenzylamine | Albidovulum sp. |
| 33 | - |
purified recombinant enzyme, pH 9.5, 65°C, substrate (S)-alpha-methylbenzylamine | Albidovulum sp. |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-alpha-methylbenzylamine + pyruvate | - |
Albidovulum sp. | acetophenone + L-alanine | - |
r | |
| (S)-alpha-methylbenzylamine + pyruvate | - |
Albidovulum sp. SLM16 | acetophenone + L-alanine | - |
r | |
| additional information | the enzyme has a clear preference for (S)-(+)-alpha-methylbenzylamine and (S)-(+)-1-methyl-3-phenylpropylamine, having the highest activity toward the former (100% relative activity). The enzyme also shows moderate activity toward aliphatic amino substrates isopropylamine and (S)-(+)-sec-butylamine, with approximately 20% and 40% of relative activity, respectively. The lowest activities (below 10% relative activity) are found when (S)-(+)-1,2,3,4-tetrahydro-1-naphtylamine and (S)-1-phenylbutylamine are used as amino donors | Albidovulum sp. | ? | - |
- |
|
| additional information | the enzyme has a clear preference for (S)-(+)-alpha-methylbenzylamine and (S)-(+)-1-methyl-3-phenylpropylamine, having the highest activity toward the former (100% relative activity). The enzyme also shows moderate activity toward aliphatic amino substrates isopropylamine and (S)-(+)-sec-butylamine, with approximately 20% and 40% of relative activity, respectively. The lowest activities (below 10% relative activity) are found when (S)-(+)-1,2,3,4-tetrahydro-1-naphtylamine and (S)-1-phenylbutylamine are used as amino donors | Albidovulum sp. SLM16 | ? | - |
- |
|
| pyruvate + (S)-1-phenylethylamine | - |
Albidovulum sp. | L-alanine + acetophenone | - |
? | |
| pyruvate + (S)-1-phenylethylamine | - |
Albidovulum sp. SLM16 | L-alanine + acetophenone | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 51170, sequence calculation, 2 * 37000, about, recombinant enzyme, SDS-PAGE | Albidovulum sp. |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| (S)-amine-transaminase | - |
Albidovulum sp. |
| (S)-ATA | - |
Albidovulum sp. |
| amine-transaminases | - |
Albidovulum sp. |
| ATA | - |
Albidovulum sp. |
| ATA_SLM16 | - |
Albidovulum sp. |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
- |
Albidovulum sp. |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
purified recombinant enzyme, pH 9.5, 80% of specific activity remaining after 5 days of incubation | Albidovulum sp. |
| 55 | - |
purified recombinant enzyme, pH 9.5, half-life is 24 h | Albidovulum sp. |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.5 | - |
- |
Albidovulum sp. |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | dependent on | Albidovulum sp. | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Albidovulum sp. | sequence calculation | - |
5.67 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | along with the structure-based classifications, a more practical system groups TAs into two groups according based on the relative position of the amino group being transferred: alpha-transaminases (alpha-TAs) and omega-transaminases (omega-TAs). While the former exclusively transfers amino groups at alpha-position relative to the carbonyl functionality (e.g. alpha-amino acids, alpha-ketoacids), the latter are able to transfer amino groups from substrates bearing it at two or more positions away from the carbonyl moiety (e.g.omega-amino acids). Depending on the selectivity, enantiopure R- and S-amines can be synthetized. This feature is derived from the two naturally occurring fold-types of transaminases, being those belonging to fold-type I known as (S)-ATAs whilst those from fold-type IV are known as (R)-ATAs. Phylogenetic analysis | Albidovulum sp. |
| additional information | homology structure modelling of ATA_SLM16 using the crystal structure of the (S)-omega-TA from chromobacterium violaceum (PDB ID 4BA5) as template | Albidovulum sp. |
| physiological function | amine-transaminases (ATAs) are enzymes that catalyze the reversible transfer of an amino group between primary amines and carbonyl compounds | Albidovulum sp. |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 55.8 | - |
(S)-alpha-methylbenzylamine | recombinant enzyme, pH 9.5, 65°C | Albidovulum sp. | |
| 96.5 | - |
pyruvate | recombinant enzyme, pH 9.5, 65°C | Albidovulum sp. | |
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