Any feedback?
Literature summary for 2.6.1.B16 extracted from
- Stereoelectronic effects in the reaction of aromatic substrates catalysed by Halomonas elongata transaminase and its mutants (2016), Org. Biomol. Chem., 14, 9306-9311 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| F84A | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| F84G | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| F84L | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| F84W | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| I258A | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| I258G | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| I258V | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| additional information | four mutants of the amine transaminase from Halomonas elongata are generated by an in silico-based design and recombinantly produced in Escherichia coli, purified, and applied to the amination of mono-substituted aromatic carbonyl-derivatives. While benzaldehyde derivatives are excellent substrates, only NO2-acetophenones are transformed into the (S)-amine with a high enantioselectivity. The different behaviour of wild-type and mutated transaminases is assessed by in silico substrate binding mode studies, overview | Halomonas elongata |
| W56A | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| W56F | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| W56G | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| W56L | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| Y149A | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| Y149F | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
| Y149G | site-directed mutagenesis, substrate specificity analysis | Halomonas elongata |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Halomonas elongata | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.06 | - |
recombinant mutant F84A, pH 8.0, 25°C | Halomonas elongata |
| 0.43 | - |
recombinant mutant I258A, pH 8.0, 25°C | Halomonas elongata |
| 0.5 | - |
recombinant mutant Y149F, pH 8.0, 25°C | Halomonas elongata |
| 3.99 | - |
recombinant wild-type enzyme, pH 8.0, 25°C | Halomonas elongata |
| 4.43 | - |
recombinant mutant W56G, pH 8.0, 25°C | Halomonas elongata |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-1-phenylethylamine + pyruvate | - |
Halomonas elongata | L-alanine + acetophenone | - |
r |  |
| 2-nitroacetophenone + L-alanine | - |
Halomonas elongata | 2-nitro-(S)-1-phenylethylamine + pyruvate | - |
r | |
| 3-nitroacetophenone + L-alanine | - |
Halomonas elongata | 3-nitro-(S)-1-phenylethylamine + pyruvate | - |
r | |
| 4-nitroacetophenone + L-alanine | - |
Halomonas elongata | 4-nitro-(S)-1-phenylethylamine + pyruvate | - |
r | |
| additional information | 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 | ? | - |
- |
|
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Halomonas elongata |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Halomonas elongata |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Halomonas elongata | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | four mutants of the amine transaminase from Halomonas elongata are generated by an in silico-based design and recombinantly produced in Escherichia coli, purified, and applied to the amination of mono-substituted aromatic carbonyl-derivatives. While benzaldehyde derivatives are excellent substrates, only NO2-acetophenones are transformed into the (S)-amine with a high enantioselectivity. The different behaviour of wild-type and mutated transaminases is assessed by in silico substrate binding mode studies, overview | Halomonas elongata |
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
