Any feedback?
Information on EC 2.6.1.B16 - amine transaminase
for references in articles please use BRENDA:EC2.6.1.B16preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.6.1.B16 amine transaminaseSpecify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
amine transaminase, (s)-selective amine transaminase, ban-ta, cv-ata, amine-transaminases, (s)-ata, ata_slm16, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-amine-transaminase
(S)-ATA
amine transaminase
amine-transaminases
ATA
ATA_SLM16
HELO 1904
HEWT
SpuC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pyruvate + (S)-1-phenylethylamine = L-alanine + acetophenone
-
-
-
-
pyruvate + (S)-1-phenylethylamine = L-alanine + acetophenone
ping-pong reaction mechanism
-
pyruvate + (S)-1-phenylethylamine = L-alanine + acetophenone
reaction mechanism for the half-transamination of L-alanine to pyruvate in (S)-selective Chromobacterium violaceum omega-transaminase by density functional theory calculations, role of a flexible arginine residue, Arg416, in the dual-substrate recognition. The amine is kinetically favored in the half-transamination of L-alanine/pyruvate, whereas the ketone is kinetically favored in the half-transamination of (S)-1-phenylethylamine/acetophenone. The arginine residue facilitates the dual-substrate recognition by functioning as an arginine switch, where the side chain is positioned inside or outside of the active site depending on the substrate. Arg416 participates in the binding of L-alanine by forming a salt bridge to the carboxylate moiety, whereas the conversion of (S)-1-phenylethylamine is feasible in the absence of Arg416, which here represents the case in which the side chain of Arg416 is positioned outside of the active site. Many PLP-dependent enzymes, including transaminases, require the formation of a so-called internal aldimine (E-PLP), before the main reaction. In this process, the PLP coenzyme becomes covalently bound to an active-site lysine residue as a protonated Schiff base, which constitutes the active form of the enzyme. The transamination reaction consists of two half-transamination equilibria. An amino donor is converted to the corresponding ketone or aldehyde, resulting in the conversion of E-PLP to pyridoxamine-5'-phosphate (PMP). The E-PLP is then regenerated by the reaction of another ketone or aldehyde, which is then converted to an amine
-
pyruvate + (S)-1-phenylethylamine = L-alanine + acetophenone
ping-pong reaction mechanism
Albidovulum sp. SLM16
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(S)-1-phenylethylamine:pyruvate aminotransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(S)-1-phenylethylamine + 4-phenyl-2-butanone
acetophenone + ?
-
-
-
r
(S)-1-phenylethylamine + methylpyruvate
acetophenone + methylalanine
-
-
-
r
(S)-1-phenylethylamine + oxaloacetate
acetophenone + L-aspartate
-
-
-
r
(S)-1-phenylethylamine + pyruvate
L-alanine + acetophenone
-
-
-
-
r
(S)-1-phenylethylamine + rac-2-methylcyclohexanone
acetophenone + ?
-
-
-
r
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
3-nitroacetophenone + L-alanine
3-nitro-(S)-1-phenylethylamine + pyruvate
-
-
-
-
r
4-nitroacetophenone + L-alanine
4-nitro-(S)-1-phenylethylamine + pyruvate
-
-
-
-
r
beta-alanine + pyruvate
4-hydroxybutyrate + L-alanine
high activity
-
-
r
isopropylamine + 4-phenylbutan-2-one
acetone + (S)-4-phenyl-2-butanamine
-
high activity, two half reaction steps, overview
-
-
r
propanal + (S)-1-phenylethylamine
propylamine + acetophenone
55% conversion of propanal
-
-
?
pyruvate + benzylamine
L-alanine + benzaldehyde
64% conversion of isopropylamine
-
-
?
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
(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
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
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
?
-
Albidovulum sp. SLM16
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
-
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
dependent on. Many PLP-dependent enzymes, including transaminases, require the formation of a so-called internal aldimine (E-PLP), before the main reaction. In this process, the PLP coenzyme becomes covalently bound to an active-site lysine residue as a protonated Schiff base, which constitutes the active form of the enzyme. The transamination reaction consists of two half-transamination equilibria. An amino donor is converted to the corresponding ketone or aldehyde, resulting in the conversion of E-PLP to pyridoxamine-5'-phosphate (PMP). The E-PLP is then regenerated by the reaction of another ketone or aldehyde, which is then converted into an amine
pyridoxal 5'-phosphate
-
PLP has a crucial role in dimerstabilization
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
additional information
additional information
-
reaction kinetics and thermodynamics of wild-type and mutant enzymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
0.0771
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A/L382M/G429A
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
33
-
purified recombinant enzyme, pH 9.5, 65°C, substrate (S)-alpha-methylbenzylamine
6
-
purified recombinant enzyme, pH 9.0, 50°C, substrate (S)-alpha-methylbenzylamine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
50
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
over 50% of maximal activity within this range, mutant enzymes ATA-v1 and ATA-v2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from a geothermal Antarctic environmental sample from a shoreline fumarole in Deception Island
-
-
brenda
Albidovulum sp. SLM16
isolated from a geothermal Antarctic environmental sample from a shoreline fumarole in Deception Island
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
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
Albidovulum sp. SLM16
-
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
Albidovulum sp. SLM16
-
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
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
Albidovulum sp. SLM16
-
homology structure modelling of ATA_SLM16 using the crystal structure of the (S)-omega-TA from chromobacterium violaceum (PDB ID 4BA5) as template
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). E1V913_HALED
Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
461
0
50423
TrEMBL
-
Q81SL2_BACAN
450
0
50286
TrEMBL
Secretory Pathway (Reliability: 2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
-
the monomer-dimer equilibrium has an effect on enzyme storage stability. After 3-4 days of incubation, the enzyme activity starts to decrease at the same time as monomers start to show up in the BN-PAGE. Cofactor has a crucial role in dimerstabilization
homodimer
-
2 * 51170, sequence calculation, 2 * 37000, about, recombinant enzyme, SDS-PAGE
homodimer
Albidovulum sp. SLM16
-
2 * 51170, sequence calculation, 2 * 37000, about, recombinant enzyme, SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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
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
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme at concentrations greater than 5mM of cofactor pyridoxal 5'-phosphate loses the activity significantly faster than 0.1mM, confirming the destabilization effect
the monomer-dimer equilibrium has an effect on enzyme storage stability. After 3-4 days of incubation, the enzyme activity starts to decrease at the same time as monomers start to show up in the BN-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
Ethanol
isopropanol
isopropyl acetate
-
the wild-type enzyme rapidly inactivates in isopropyl acetate, while enzyme mutants ATA-v1 and ATA-v2 are more stable, overview
Methanol
tert-Butanol
toluene
-
the wild-type enzyme rapidly inactivates in toluene, while enzyme mutants ATA-v1 and ATA-v2 are more stable, overview
additional information
additional information
-
the recombinant enzyme shows good stability in the presence of organic solvents
additional information
Albidovulum sp. SLM16
-
the recombinant enzyme shows good stability in the presence of organic solvents
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20-4°C, purified recombinant enzyme in 50 mM HEPES, pH 8.2, stored for six months in 50% glycerol is still fully active (114%) and the same solution stored at room temperature maintains 77% activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli BL21(DE3) by nickel affinity chromatography and desalting gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ata_slm16, Phylogenetic analysis, functional recombinant overexpression in Escherichia coli strain BL21 (C2530)
-
recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in transformed phage-resistant Escherichia coli strain BL21(DE3)
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli BL21(DE3)
-
recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in transformed phage-resistant Escherichia coli strain BL21(DE3)
-
recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in transformed phage-resistant Escherichia coli strain BL21(DE3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
amine transaminase (ATA) catalyzing stereoselective amination of prochiral ketones is an attractive alternative to transition metal catalysis
synthesis
-
the covalently immobilized enzyme is used for amine bioproduction in batch and flow reaction systems, method evaluation, overview. Produced vanillylamine is a valuable building block for the synthesis of natural products, such as capsaicinoids
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.6.1.B16)
html completed
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)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
