EC Number   |
Substrates |
Organism |
Products |
Reversibility  |
|---|
   2.6.1.B16 | more |
application of the amine transaminase (ATA) for stereoselective amination of prochiral ketones represents an environmentally benign and economically attractive alternative to transition metal catalyzed asymmetric synthesis, overview |
Chromobacterium violaceum |
? |
- |
- |
| 2.6.1.B16 | more |
engineered ATAs perform asymmetric synthesis of the respective R-amine with high conversions by using either alanine or isopropylamine as amine donor. Asymmetric synthesis of (R)-2,2-dimethyl-1-phenylpropan-1-amine by amino group transfer to 2,2-dimethyl-1-phenylpropan-1-one catalyzed by ATAs. Isopropylamine or alanine serve as the amine donors. Analysis of specific activities of Rsp-ATA mutant variants towards rac-amine 2,2-dimethyl-1-phenylpropan-1-amine. Enzyme-ligand interaction analysis, overview |
Ruegeria sp. TM1040 |
? |
- |
- |
| 2.6.1.B16 | more |
substrate specificity of Ban-TA, overview. Even though enzyme Ban-TA shows a relatively narrow amine substrate scope within the tested substrates, it accepts 2-propylamine, which is a prerequisite for industrial asymmetric amine synthesis. Structural information imply that the so-called dual substrate recognition of chemically different substrates (i.e. amines and amino acids) differs from that in formerly known enzymes. It lacks the normally conserved flipping arginine, which enables dual substrate recognition by its side chain flexibility in other omega-amino acid:pyruvate transaminases. Molecular dynamics studies suggest that another arginine (R162) binds omega-amino acids in Ban-TA, but no side chain movements are required for amine and amino acid binding |
Bacillus anthracis |
? |
- |
- |
| 2.6.1.B16 | more |
substrate specificity of wild-type and mutant enzymes, overview. No activity of mutant F84G with (S)-1-phenylethylamine. Analysis of activity of the enzymes with ortho-, meta-, and para-substituted derivatives of fluoroacetophenone, trifluoroacetophenone, methoxyacetophenone, methylacetophenone, nitrobenzaldehyde, fluorobenzaldehyde, trifluorobenzaldehyde, methoxybenzaldehyde, methylbenzaldehyde, and of benzaldehyde, docking study |
Halomonas elongata |
? |
- |
- |
| 2.6.1.B16 | more |
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. |
? |
- |
- |
| 2.6.1.B16 | more |
vanillylamine is a valuable building block for the synthesis of natural products, such as capsaicinoids |
Halomonas elongata |
? |
- |
- |
| 2.6.1.B16 | more |
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 |
? |
- |
- |
| 2.6.1.B16 | (S)-(-)-1-phenyl-ethylamine + 4-nitrobenzaldehyde |
complete conversion at pH 8.0 and 37°C |
Halomonas elongata |
4-nitrobenzylamine + L-alanine |
- |
? |
| 2.6.1.B16 | (S)-(-)-1-phenyl-ethylamine + cinnamaldehyde |
- |
Halomonas elongata |
cinnamylamine + L-alanine |
- |
? |
| 2.6.1.B16 | (S)-(-)-1-phenyl-ethylamine + vanillin |
- |
Halomonas elongata |
vanillylamine + L-alanine |
- |
? |
