2.6.1.B16: amine transaminase
This is an abbreviated version!
For detailed information about amine transaminase, go to the full flat file.
Word Map on EC 2.6.1.B16
Reaction
Synonyms
(S)-amine-transaminase, (S)-ATA, (S)-selective amine transaminase, (S)-selective Chromobacterium violaceum omega-transaminase, (S)-selective omega-transaminase, amine transaminase, amine-transaminases, ATA, ATA_SLM16, Ban-TA, Cv-ATA, Cv-omegaTA, HELO 1904, HEWT, omega-amino acid:pyruvate transaminase, omega-TA, omega-transaminase, Rsp-ATA, SpuC
ECTree
2.6.1.B16 amine transaminaseAdvanced search results
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results (Engineering
Engineering on EC 2.6.1.B16 - amine transaminase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R162A
site-directed mutagenesis, compared to wild-type, activities of the R162 mutant drop around ten times if the reaction comprises carboxylic substrates, e.g. when (S)-PEA is employed with pyruvate or succinic semialdehyde as substrates
R410A
site-directed mutagenesis, the mutant converts all tested substrate combinations with similar or slightly higher activity compared to wild-type
P281S
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site-directed mutagenesis, the mutation seems to have a negative effect on specific activity
Y152F
-
site-directed mutagenesis, the mutation stabilizes the enzyme, the activity is slightly reduced compared to wild-type
Y59W/Y87L/T231A
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site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type
Y59W/Y87L/T231A/G429A
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site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type
Y59W/Y87L/T231A/L382M
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site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type
Y59W/Y87L/T231A/L382M/G429A
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site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type
Y59W/Y87L/Y152F/T231A/L382M/G429A
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site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type
G51S
-
site-directed mutagenesis, the ATA-v2 mutant shows superior operational, temperature and solvent stability as well as improved activity for the pharmaceutical relevant amine product 4-phenyl-2-butanamine appears to be specific for thermal tolerance, compared to wild-type, mutant ATA-v1 shows increased temperature optimum, and features excellent operational stability in biphasic (aqueous/nonpolar solvent) reaction systems at 45°C, when the aqueous phase contained an approximate amine donor-to-acceptor ratio
N161I/Y164L
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site-directed mutagenesis, double mutant ATA-v1 with two point mutations in the cofactor-ring motif shows superior operational, temperature and solvent stability as well as improved activity for the pharmaceutical relevant amine product 4-phenyl-2-butanamine, while the enantioselectivity for (S)-PBA is raised from 59 to 96%, compared to the wild-type enzyme. Compared to wild-type, mutant ATA-v1 shows increased temperature optimum, and features excellent operational stability in biphasic (aqueous/nonpolar solvent) reaction systems at 45°C, when the aqueous phase contained an approximate amine donor-to-acceptor ratio of 50:1. In contrast to wild-type ATA, ATA-v1 seems to resist denaturation upon interfacial contact under turbulent conditions. ATA-v1 appears to slightly gain activity with time in the presence of n-heptane and toluene
additional information
additional information
comparison of pH-profile and amino acceptor substrate specificity of mutants R162A and R410A and wild-type Ban-TA
additional information
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development of an efficient bioproduction of amines by exploiting the immobilised (S)-selective amine transaminase from Halomonas elongata (HEWT), which shows a very broad substrate scope, tolerating a range of temperatures, pH values, salts, and co-solvents, in a continuous flow-reactor. The immobilised HEWT (imm-HEWT) is applied to continuous-flow reactions maintaining the biocatalyst in a packed-bed reactor to decrease reaction times and increase the productivity. The addition of an in-line purification step allows for the recovery of the pure products without any additional work-up procedure. Method optimization and evaluation, overview
additional information
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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
additional information
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mutational analysis of enzyme-substrate interactions and substrate specificity, overview
additional information
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semi-rational mutagenesis study for enzymes with higher activity and higher selectivity, employing the proprietary multi-dimensional-mutagenesis (MDM) and automated generation of mutant (AGM) technologies (c-LEcta)
