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
results (
results (Substrates Products
Substrates Products on EC 2.6.1.B16 - amine transaminase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
-
-
-
