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(S)-(-)-1-phenyl-ethylamine + 4-nitrobenzaldehyde
4-nitrobenzylamine + L-alanine
-
complete conversion at pH 8.0 and 37°C
-
-
?
(S)-(-)-1-phenyl-ethylamine + cinnamaldehyde
cinnamylamine + L-alanine
-
-
-
-
?
(S)-(-)-1-phenyl-ethylamine + vanillin
vanillylamine + L-alanine
-
-
-
-
?
(S)-1-phenylethylamine + 2-butanone
acetophenone + ?
-
-
-
r
(S)-1-phenylethylamine + 2-heptanone
acetophenone + ?
-
-
-
r
(S)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(S)-1-phenylethylamine + 4-phenyl-2-butanone
acetophenone + ?
-
-
-
r
(S)-1-phenylethylamine + beta-tetralone
acetophenone + ?
-
-
-
r
(S)-1-phenylethylamine + cyclohexanone
acetophenone + ?
-
-
-
r
(S)-1-phenylethylamine + cyclooctanone
acetophenone + ?
-
-
-
r
(S)-1-phenylethylamine + methoxyacetone
acetophenone + ?
-
-
-
r
(S)-1-phenylethylamine + methylpyruvate
acetophenone + methylalanine
-
-
-
r
(S)-1-phenylethylamine + oxaloacetate
acetophenone + L-aspartate
-
-
-
r
(S)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(S)-1-phenylethylamine + pyruvate
L-alanine + acetophenone
-
-
-
-
r
(S)-1-phenylethylamine + rac-2-methylcyclohexanone
acetophenone + ?
-
-
-
r
(S)-alpha-methylbenzylamine + pyruvate
acetophenone + L-alanine
2,2-dimethyl-1-phenylpropan-1-one + isopropylamine
(R)-2,2-dimethyl-1-phenylpropan-1-amine + acetone
-
the conversion by all active enzyme mutants lays between 22 and 71% with isopropylamine as amine donor, with enantiomeric excess above 99%, low activity
-
-
r
2,2-dimethyl-1-phenylpropan-1-one + L-alanine
(R)-2,2-dimethyl-1-phenylpropan-1-amine + pyruvate
-
the conversion by all active enzyme mutants is complete with L-alanine as amine donor, with enantiomeric excess above 99%
-
-
r
2-nitroacetophenone + L-alanine
2-nitro-(S)-1-phenylethylamine + pyruvate
-
-
-
-
r
2-phenylpropionaldehyde + (S)-1-phenylethylamine
2-phenylpropylamine + acetophenone
3-nitroacetophenone + L-alanine
3-nitro-(S)-1-phenylethylamine + pyruvate
-
-
-
-
r
4-nitroacetophenone + L-alanine
4-nitro-(S)-1-phenylethylamine + pyruvate
-
-
-
-
r
benzaldehyde + ortho-xylylenediamine
benzylamine + ?
beta-alanine + pyruvate
4-hydroxybutyrate + L-alanine
high activity
-
-
r
cinnamaldehyde + (S)-1-phenylethylamine
(2E)-3-phenylprop-2-en-1-amine + acetophenone
isopropylamine + 4-phenylbutan-2-one
acetone + (S)-4-phenyl-2-butanamine
-
high activity, two half reaction steps, overview
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
propanal + (S)-1-phenylethylamine
propylamine + acetophenone
55% conversion of propanal
-
-
?
pyruvate + (S)-1-phenylethylamine
L-alanine + acetophenone
pyruvate + benzylamine
L-alanine + benzaldehyde
64% conversion of isopropylamine
-
-
?
pyruvate + glycine
L-alanine + glyoxylate
pyruvate + isopropylamine
L-alanine + acetone
41% conversion of isopropylamine
-
-
?
pyruvate + L-serine
L-alanine + 3-hydroxy-2-oxopropanoate
19% conversion of serine
-
-
?
rac-2,2-dimethyl-1-phenylpropan-1-amine + pyruvate
2,2-dimethyl-1-phenylpropan-1-one + L-alanine
-
-
-
-
r
additional information
?
-
(S)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
-
-
-
r
(S)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
-
-
-
-
r
(S)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
-
mechanism of the conversion of (S)-1-phenylethylamine to acetophenone, overview
-
-
r
(S)-alpha-methylbenzylamine + pyruvate
acetophenone + L-alanine
-
-
-
-
r
(S)-alpha-methylbenzylamine + pyruvate
acetophenone + L-alanine
-
-
-
-
r
2-phenylpropionaldehyde + (S)-1-phenylethylamine
2-phenylpropylamine + acetophenone
67% conversion of 2-phenylpropionaldehyde
-
-
?
2-phenylpropionaldehyde + (S)-1-phenylethylamine
2-phenylpropylamine + acetophenone
67% conversion of 2-phenylpropionaldehyde
-
-
?
benzaldehyde + ortho-xylylenediamine
benzylamine + ?
95% conversion of benzaldehyde
conversion rate 90-95%
-
?
benzaldehyde + ortho-xylylenediamine
benzylamine + ?
95% conversion of benzaldehyde
conversion rate 90-95%
-
?
cinnamaldehyde + (S)-1-phenylethylamine
(2E)-3-phenylprop-2-en-1-amine + acetophenone
56% conversion of cinnamaldehyde
-
-
?
cinnamaldehyde + (S)-1-phenylethylamine
(2E)-3-phenylprop-2-en-1-amine + acetophenone
56% conversion of cinnamaldehyde
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
41% conversion of alanine, 97% conversion of glyoxylate
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
41% conversion of alanine, 97% conversion of glyoxylate
-
-
?
pyruvate + (S)-1-phenylethylamine
L-alanine + acetophenone
-
-
-
-
?
pyruvate + (S)-1-phenylethylamine
L-alanine + acetophenone
-
-
-
-
?
pyruvate + (S)-1-phenylethylamine
L-alanine + acetophenone
97% conversion of (S)-1-phenylethylamine, less than 5% conversion of (R)-1-phenylethylamine
-
-
?
pyruvate + glycine
L-alanine + glyoxylate
97% conversion of pyruvate
-
-
?
pyruvate + glycine
L-alanine + glyoxylate
97% conversion of pyruvate
-
-
?
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
-
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
vanillylamine is a valuable building block for the synthesis of natural products, such as capsaicinoids
-
-
-
additional information
?
-
-
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
-
-
-
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0.0016
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and 4-phenyl-2-butanone
0.0018
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and rac-2-methylcyclohexanone
0.0019
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and 2-heptanone
0.002
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and cyclohexanone
0.0021
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and 2-butanone
0.0028
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and methoxyacetone
0.0038
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and cyclooctanone
0.0065
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87V/T231A
0.0067
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and beta-tetralone
0.007
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and oxaloacetate
0.0115
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A
0.019
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A/L382M
0.0324
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A/P281S/G429A
0.0448
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A/G429A
0.06
-
recombinant mutant F84A, pH 8.0, 25°C
0.0771
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A/L382M/G429A
0.43
-
recombinant mutant I258A, pH 8.0, 25°C
0.5
-
recombinant mutant Y149F, pH 8.0, 25°C
0.58
substrate benzaldehyde, cosubstrate isopropylamine, pH 8.0, 37°C
0.94
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and pyruvate or methylpyruvate
1.3
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates (S)-1-phenylethylamine and 2-oxoglutarate
2.5
purified recombinant wild-type enzyme, pH 10.0, 30°C, substrates beta-alanine and pyruvate
3.99
-
recombinant wild-type enzyme, pH 8.0, 25°C
33
-
purified recombinant enzyme, pH 9.5, 65°C, substrate (S)-alpha-methylbenzylamine
4.43
-
recombinant mutant W56G, pH 8.0, 25°C
6
-
purified recombinant enzyme, pH 9.0, 50°C, substrate (S)-alpha-methylbenzylamine
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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
evolution
-
the ATA enzyme from Ruegeria sp. TM1040 (Rsp-ATA, PDB ID 3FCR) belongs to the ATAs of fold class I
evolution
the enzyme belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family
evolution
-
the enzyme has a high sequence identity to a fold type I class III transaminase from Pseudomonas fluorescens
evolution
-
there are two types of TAs, alpha-transaminases, which convert alpha-amino and alpha-keto acids, and omega-transaminases (omegaTAs), which also accept amino and keto acids in which the amino or keto group is in a non-alpha position relative to the carboxyl group, called omega-amino or omega-keto acids, respectively
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
-
physiological function
-
amine-transaminases (ATAs) are enzymes that catalyze the reversible transfer of an amino group between primary amines and carbonyl compounds
physiological function
-
transaminases (TAs) catalyze the reversible interchange of amino and keto groups, by the use of the coenzyme pyridoxal-5'-phosphate (PLP)
physiological function
-
transaminases play a central role in the biocatalytic preparation of enantiopure amines and amino acids, challenging reactions to achieve by conventional synthesis
physiological function
-
amine-transaminases (ATAs) are enzymes that catalyze the reversible transfer of an amino group between primary amines and carbonyl compounds
-
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
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
additional information
-
quantum chemical study of dual-substrate recognition in omega-transaminase. The reaction mechanism for the half-transamination of L-alanine to pyruvate in (S)-selective Chromobacterium violaceum omega-transaminase is investigated using density functional theory calculations. The role of a flexible arginine residue, Arg416, in the dual-substrate recognition is revealed using two different active site models, one including this residue and one lacking it. Molecular docking and molecular dynamics simulations, active site modeling, overview. The amino acids that make up the binding site are Phe22, Leu59, Trp60, Phe88', Tyr153, Ile262, and Thr321', as well as Gly230 and Ala231 and the backbone between them
additional information
-
sequence-structure-function relationship
additional information
structure-function analysis, molecular dynamics simulations, and molecular modeling of substrate recognition. Residue W56 is the only residue in direct contact with alanine's carboxylate. Residue R162, pointing towards the substrate from the active site's entrance is binding the carboxylate indirectly via two water molecules
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
-
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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
F84A
-
site-directed mutagenesis, substrate specificity analysis
F84G
-
site-directed mutagenesis, substrate specificity analysis
F84L
-
site-directed mutagenesis, substrate specificity analysis
F84W
-
site-directed mutagenesis, substrate specificity analysis
I258A
-
site-directed mutagenesis, substrate specificity analysis
I258G
-
site-directed mutagenesis, substrate specificity analysis
I258V
-
site-directed mutagenesis, substrate specificity analysis
W56A
-
site-directed mutagenesis, substrate specificity analysis
W56F
-
site-directed mutagenesis, substrate specificity analysis
W56G
-
site-directed mutagenesis, substrate specificity analysis
W56L
-
site-directed mutagenesis, substrate specificity analysis
Y149A
-
site-directed mutagenesis, substrate specificity analysis
Y149F
-
site-directed mutagenesis, substrate specificity analysis
Y149G
-
site-directed mutagenesis, substrate specificity analysis
P281S
-
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/T231A
-
site-directed mutagenesis, inactive mutant
Y59W/Y87F/T231A
-
site-directed mutagenesis, inactive mutant
Y59W/Y87L/T231A
-
site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type
Y59W/Y87L/T231A/G429A
-
site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type
Y59W/Y87L/T231A/L382M
-
site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type
Y59W/Y87L/T231A/L382M/G429A
-
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
-
site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type
Y59W/Y87V/T231A
-
site-directed mutagenesis
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
-
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
comparison of pH-profile and amino acceptor substrate specificity of mutants R162A and R410A and wild-type Ban-TA
additional information
-
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
-
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
-
mutational analysis of enzyme-substrate interactions and substrate specificity, overview
additional information
-
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)
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35
24 h, stable up to 35°C
50
-
purified recombinant enzyme, pH 9.5, 80% of specific activity remaining after 5 days of incubation
50 - 62
-
wild-type enzyme, completely stable up to 55°C, loss of 50% activity at 60°C, inactivation at 62°C
50 - 75
-
enzyme mutant ATA-v1, completely stable up to 70°C, loss of 50% activity at 71°C, inactivation at 75°C
50 - 78
-
enzyme mutant ATA-v2, completely stable up to 72°C, loss of 50% activity at 74°C, inactivation at 78°C
55
-
purified recombinant enzyme, pH 9.5, half-life is 24 h
78
-
the enzyme displays a high Tm of 78°C in 100 mM HEPES, pH 7.4, and 100 mM NaCl
additional information
-
effects of co-solvents, i.e. DMSO, glycerol, and methanol, as well as of NaCl and sucrose on the Tm value of the enzyme, overview. DMSO, NaCl, and methanol, and also phenylethylamine and L-alanine reduce the Tm value, while pyruvate, glycerol, and sucrose increase it. The addition of amine substrates (L-alanine and (S)-1-PEA) displaying destabilizing effects may result from PMP (the reduced amine form of the cofactor PLP) formation. PMP is not covalently bound to the enzyme's active site and may therefore promote enzyme destabilization or denaturation
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Cerioli, L.; Planchestainer, M.; Cassidy, J.; Tessaro, D.; Paradisi, F.
Characterization of a novel amine transaminase from Halomonas elongata
J. Mol. Catal. B
120
141-150
2015
Halomonas elongata (E1V913), Halomonas elongata DSM 2581 (E1V913)
-
brenda
Manta, B.; Cassimjee, K.; Himo, F.
Quantum chemical study of dual-substrate recognition in omega-transaminase
ACS Omega
2
890-898
2017
Chromobacterium violaceum
brenda
Steffen-Munsberg, F.; Matzel, P.; Sowa, M.; Berglund, P.; Bornscheuer, U.; Hoehne, M.
Bacillus anthracis omega-amino acid pyruvate transaminase employs a different mechanism for dual substrate recognition than other amine transaminases
Appl. Microbiol. Biotechnol.
100
4511-4521
2016
uncultured bacterium, Bacillus anthracis (Q81SL2)
-
brenda
Weiss, M.S.; Pavlidis, I.V.; Spurr, P.; Hanlon, S.P.; Wirz, B.; Iding, H.; Bornscheuer, U.T.
Amine transaminase engineering for spatially bulky substrate acceptance
ChemBioChem
18
1022-1026
2017
Ruegeria sp. TM1040
brenda
Marquez, S.L.; Atalah, J.; Blamey, J.M.
Characterization of a novel thermostable (S)-amine-transaminase from an Antarctic moderately-thermophilic bacterium Albidovulum sp. SLM16
Enzyme Microb. Technol.
131
109423
2019
Albidovulum sp., Albidovulum sp. SLM16
brenda
Payer, S.; Schrittwieser, J.; Kroutil, W.
Vicinal diamines as smart cosubstrates in the transaminase-catalyzed asymmetric amination of ketones
Eur. J. Org. Chem.
2017
2553-2559
2017
Chromobacterium violaceum
-
brenda
Planchestainer, M.; Contente, M.; Cassidy, J.; Molinari, F.; Tamborini, L.; Paradisi, F.
Continuous flow biocatalysis Production and in-line purification of amines by immobilised transaminase from Halomonas elongata
Green Chem.
19
372-375
2017
Halomonas elongata
-
brenda
Contente, M.L.; Planchestainer, M.; Molinari, F.; Paradisi, F.
Stereoelectronic effects in the reaction of aromatic substrates catalysed by Halomonas elongata transaminase and its mutants
Org. Biomol. Chem.
14
9306-9311
2016
Halomonas elongata
brenda