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(R)-1-phenylethylamine + 2-oxoisocaproate
acetophenone + D-leucine
-
-
-
-
r
(R)-1-phenylethylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
(R)-1-phenylethylamine + pyruvate
acetophenone + D-alanine
-
-
-
-
r
(R)-alpha-ethylbenzylamine + 3-methyl-2-oxovalerate
alpha-ethylbenzaldehyde + L-isoleucine
reaction of (R)-amine:pyruvate transaminase, EC 2.6.1.B21
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-
r
(R)-alpha-ethylbenzylamine + pyruvate
alpha-ethylbenzaldehyde + D-alanine
R-EtBA
-
-
r
(R)-alpha-methylbenzylamine + 2-oxobutyrate
acetophenone + L-alpha-aminobutyric acid
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + L-glutamate
(R)-alpha-methylbenzylamine + 2-oxohexanoate
acetophenone + L-norleucine
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxovalerate
acetophenone + L-norvaline
-
-
-
r
(R)-alpha-methylbenzylamine + 3-methyl-2-oxobutyrate
acetophenone + L-valine
-
-
-
r
(R)-alpha-methylbenzylamine + 3-methyl-2-oxovalerate
acetophenone + D-isoleucine
-
-
-
r
(R)-alpha-methylbenzylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
(R)-alpha-methylbenzylamine + 4-methyl-2-oxovalerate
acetophenone + L-leucine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + L-alanine
2,2-dimethyl-1-phenyl-propan-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
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-
r
2,2-dimethyl-1-phenyl-propan-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-oxo-4-hydroxybutyrate + isopropylamine
D-homoserine + acetone
-
low activity, 6% activity compared to pyruvate
-
-
r
2-oxo-hexanoate + isopropylamine
D-norleucine + acetone
-
low activity, 2% activity compared to pyruvate
-
-
r
2-oxobutyrate + isopropylamine
D-2-aminobutyrate + acetone
-
33% activity compared to pyruvate
-
-
r
2-oxohexanoate + L-glutamate
norleucine + 2-oxoglutarate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
2-oxovalerate + isopropylamine
D-2-amino-pentanoate + acetone
-
low activity, 2% activity with 2b compared to pyruvate
-
-
r
D-alanine + 2-oxoglutarate
pyruvate + D-glutamate
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + D-glutamate
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
pyruvate + isopropylamine
D-alanine + acetone
-
-
-
-
r
rac-2,2-dimethyl-1-phenylpropan-1-amine + pyruvate
2,2-dimethyl-1-phenyl-propan-1-one + L-alanine
-
-
-
-
r
additional information
?
-
(R)-1-phenylethylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
the enzyme is active towards (R)-PEA and not active towards (S)-PEA
-
-
r
(R)-1-phenylethylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
the enzyme is active towards (R)-PEA and not active towards (S)-PEA
-
-
r
(R)-1-phenylethylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
the enzyme is active towards (R)-PEA and not active towards (S)-PEA
-
-
r
(R)-1-phenylethylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
the enzyme is active towards (R)-PEA and not active towards (S)-PEA
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
low activity
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
low activity
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
low activity
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
low activity
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
low activity
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
low activity
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
low activity
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + L-glutamate
reaction of (R)-amine:pyruvate transaminase, EC 2.6.1.B21
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-
r
(R)-alpha-methylbenzylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
-
-
-
r
(R)-alpha-methylbenzylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
reaction of (R)-amine:pyruvate transaminase, EC 2.6.1.B21
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-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor
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-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
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-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor
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-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
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-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
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-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
R-MBA, specific substrate for (R)-amine:pyruvate transaminases
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-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + L-alanine
-
-
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + L-alanine
-
isopropylamine is one of the preferred amino donors for omega-TA
-
-
r
D-alanine + 2-oxoglutarate
pyruvate + D-glutamate
-
-
-
r
D-alanine + 2-oxoglutarate
pyruvate + D-glutamate
very low activity, reaction of EC 2.6.1.21
-
-
r
D-alanine + 2-oxoglutarate
pyruvate + D-glutamate
very low activity, reaction of EC 2.6.1.21
-
-
r
D-alanine + 2-oxoglutarate
pyruvate + D-glutamate
very low activity, reaction of EC 2.6.1.21
-
-
r
D-alanine + 2-oxoglutarate
pyruvate + D-glutamate
very low activity, reaction of EC 2.6.1.21
-
-
r
D-alanine + 2-oxoglutarate
pyruvate + D-glutamate
very low activity, reaction of EC 2.6.1.21
-
-
r
D-alanine + 2-oxoglutarate
pyruvate + D-glutamate
very low activity, reaction of EC 2.6.1.21
-
-
r
D-alanine + 2-oxoglutarate
pyruvate + D-glutamate
very low activity, reaction of EC 2.6.1.21
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + D-glutamate
reaction of EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + D-glutamate
reaction of EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + D-glutamate
reaction of EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + D-glutamate
reaction of EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + D-glutamate
reaction of EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + D-glutamate
reaction of EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + D-glutamate
reaction of EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
additional information
?
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-
developed of a deracemization method for production of D-amino acids using L-alanine dehydrogenase (AlaDH), D-selective omega-transaminase (omega-TA) ARTAmut, and NADH oxidase (NOX). Unwanted L-amino acid in the racemic mixture is converted to a D-form after two consecutive reactions catalyzed by AlaDH and ARTA mut, leading to complete deracemization or enantioenrichment depending on the substrate specificity of the two enzymes, reaction cascade and method evaluation, overview
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-
additional information
?
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(R)-amination mediated by (R)-specific omega-transaminases generally requires costly D-alanine in excess to obtain the desired chiral amines in high yield. A one-pot, trienzymatic cascade comprising an (R)-specific omega-transaminase, an amine dehydrogenase, and a formate dehydrogenase is developed for the economical and ecofriendly synthesis of (R)-chiral amines. Using inexpensive ammonium formate as the sole sacrificial agent, the established cascade system enables efficient omega-transaminase-mediated (R)-amination of various ketones, with high conversions and excellent enantiomeric excess (over 99%), water and CO2 are the only waste products. The wild-type enzyme shows broad substrate specificity and enantioselectivity. Cascade reaction, overview
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-
-
additional information
?
-
(R)-amination mediated by (R)-specific omega-transaminases generally requires costly D-alanine in excess to obtain the desired chiral amines in high yield. A one-pot, trienzymatic cascade comprising an (R)-specific omega-transaminase, an amine dehydrogenase, and a formate dehydrogenase is developed for the economical and ecofriendly synthesis of (R)-chiral amines. Using inexpensive ammonium formate as the sole sacrificial agent, the established cascade system enables efficient omega-transaminase-mediated (R)-amination of various ketones, with high conversions and excellent enantiomeric excess (over 99%), water and CO2 are the only waste products. The wild-type enzyme shows broad substrate specificity and enantioselectivity. Cascade reaction, overview
-
-
-
additional information
?
-
(R)-amination mediated by (R)-specific omega-transaminases generally requires costly D-alanine in excess to obtain the desired chiral amines in high yield. A one-pot, trienzymatic cascade comprising an (R)-specific omega-transaminase, an amine dehydrogenase, and a formate dehydrogenase is developed for the economical and ecofriendly synthesis of (R)-chiral amines. Using inexpensive ammonium formate as the sole sacrificial agent, the established cascade system enables efficient omega-transaminase-mediated (R)-amination of various ketones, with high conversions and excellent enantiomeric excess (over 99%), water and CO2 are the only waste products. The wild-type enzyme shows broad substrate specificity and enantioselectivity. Cascade reaction, overview
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-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bthu also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bthu shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
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-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bthu also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bthu shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
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-
-
additional information
?
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the forward reaction is preferred. Enzyme R-omegaAT_Bthu mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
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-
-
additional information
?
-
the forward reaction is preferred. Enzyme R-omegaAT_Bthu mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
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-
-
additional information
?
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-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
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-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
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-
-
additional information
?
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-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
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-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses BCAT activity (EC 2.6.1.42). No activity with (S)-alpha-methylbenzylamine and D-alanine
-
-
-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows very low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
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-
additional information
?
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enzyme Hoch3033 is a transaminases with a n enzyme with mixed type of activity showing branched-chain amino acid amintransferase activity (EC 2.6.1.42) and (R)-amine:pyruvate transaminase (EC 2.6.1). The mixed type of activity of Hoch3033 is implemented within the BCAT-like active site, but in the active site of Hoch3033, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. In the standard assay, the specific activity towards (S)-alpha-methylbenzylamine (S-MBA) is only 0.32% of the activity towards R-MBA. A much lower value of activity is obtained with (R)-alpha-ethylbenzylamine (R-EtBA), the closest homologue of R-MBA. No activity towards S-EtBA is observed. Substrate specificity overview
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-
additional information
?
-
enzyme Hoch3033 is a transaminases with a n enzyme with mixed type of activity showing branched-chain amino acid amintransferase activity (EC 2.6.1.42) and (R)-amine:pyruvate transaminase (EC 2.6.1). The mixed type of activity of Hoch3033 is implemented within the BCAT-like active site, but in the active site of Hoch3033, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. In the standard assay, the specific activity towards (S)-alpha-methylbenzylamine (S-MBA) is only 0.32% of the activity towards R-MBA. A much lower value of activity is obtained with (R)-alpha-ethylbenzylamine (R-EtBA), the closest homologue of R-MBA. No activity towards S-EtBA is observed. Substrate specificity overview
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-
additional information
?
-
no activity with 2-oxoglutarate and with beta-Ala and D-Ala. The deamination of L-Leu and L-Ile by the transaminase from Haliangium ochraceum is observed only in half-reactions. Reaction mechanisms
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additional information
?
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the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
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additional information
?
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the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
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additional information
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no activity with 2-oxoglutarate and with beta-Ala and D-Ala. The deamination of L-Leu and L-Ile by the transaminase from Haliangium ochraceum is observed only in half-reactions. Reaction mechanisms
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additional information
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no activity with 2-oxoglutarate and with beta-Ala and D-Ala. The deamination of L-Leu and L-Ile by the transaminase from Haliangium ochraceum is observed only in half-reactions. Reaction mechanisms
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additional information
?
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no activity with 2-oxoglutarate and with beta-Ala and D-Ala. The deamination of L-Leu and L-Ile by the transaminase from Haliangium ochraceum is observed only in half-reactions. Reaction mechanisms
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additional information
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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-phenyl-propan-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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additional information
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besides R-omegaAT activity, the enzyme R-omegaAT_Sery also possesses D-alanine aminotransferase (DAT, EC 2.6.1.21) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. No BCAT activity (EC 2.6.1.42) is observed for enzyme R-omegaAT_Sery, no activity with L-leucine
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additional information
?
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besides R-omegaAT activity, the enzyme R-omegaAT_Sery also possesses D-alanine aminotransferase (DAT, EC 2.6.1.21) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. No BCAT activity (EC 2.6.1.42) is observed for enzyme R-omegaAT_Sery, no activity with L-leucine
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additional information
?
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the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses DAT activity (EC 2.6.1.21). No activity with (S)-alpha-methylbenzylamine and L-leucine
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additional information
?
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the forward reaction is preferred. Enzyme R-omegaAT_Sery mainly possesses DAT activity (EC 2.6.1.21). No activity with (S)-alpha-methylbenzylamine and L-leucine
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additional information
?
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besides R-omegaAT activity, the enzyme R-omegaAT_Sery also possesses D-alanine aminotransferase (DAT, EC 2.6.1.21) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. No BCAT activity (EC 2.6.1.42) is observed for enzyme R-omegaAT_Sery, no activity with L-leucine
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additional information
?
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besides R-omegaAT activity, the enzyme R-omegaAT_Sery also possesses D-alanine aminotransferase (DAT, EC 2.6.1.21) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. No BCAT activity (EC 2.6.1.42) is observed for enzyme R-omegaAT_Sery, no activity with L-leucine
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additional information
?
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besides R-omegaAT activity, the enzyme R-omegaAT_Sery also possesses D-alanine aminotransferase (DAT, EC 2.6.1.21) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. No BCAT activity (EC 2.6.1.42) is observed for enzyme R-omegaAT_Sery, no activity with L-leucine
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additional information
?
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besides R-omegaAT activity, the enzyme R-omegaAT_Sery also possesses D-alanine aminotransferase (DAT, EC 2.6.1.21) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. No BCAT activity (EC 2.6.1.42) is observed for enzyme R-omegaAT_Sery, no activity with L-leucine
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additional information
?
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besides R-omegaAT activity, the enzyme R-omegaAT_Sery also possesses D-alanine aminotransferase (DAT, EC 2.6.1.21) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. No BCAT activity (EC 2.6.1.42) is observed for enzyme R-omegaAT_Sery, no activity with L-leucine
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additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Sery also possesses D-alanine aminotransferase (DAT, EC 2.6.1.21) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. No BCAT activity (EC 2.6.1.42) is observed for enzyme R-omegaAT_Sery, no activity with L-leucine
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0.0065
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pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87V/T231A
0.008
-
pH 9.0, 30°C, substrate (R)-1-phenylethylamine, recombinant enzyme mutant Y31F
0.0115
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pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A
0.012
-
pH 9.0, 30°C, substrate (R)-1-phenylethylamine, recombinant enzyme mutant Y88E
0.013
purified recombinant enzyme, pH 10.0, 40°C, substrate (R)-alpha-ethylbenzylamine and 3-methyl-2-oxovalerate
0.0183
-
pH 9.0, 30°C, substrate (R)-1-phenylethylamine, recombinant enzyme mutant M2-4
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
0.041
-
pH 9.0, 30°C, substrate (R)-1-phenylethylamine, recombinant enzyme mutant M2-3
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
0.1
purified recombinant enzyme, pH 9.0, 40°C, substrates (R)-1-phenylethylamine and 3-methyl-3-oxovalerate
0.185
-
pH 9.0, 30°C, substrate (R)-1-phenylethylamine, recombinant enzyme mutant M2-5
0.326
-
pH 9.0, 30°C, substrate (R)-1-phenylethylamine, recombinant enzyme mutant M2-6
0.000087
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and 2-oxoglutarate
0.000087
purified recombinant enzyme, substrates (R)-alpha-methylbenzylamine and 2-oxoglutarate, pH and temperature not specified in the publication
0.00022
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and pyruvate
0.00022
purified recombinant enzyme, substrates (R)-alpha-methylbenzylamine and pyruvate, pH and temperature not specified in the publication
0.00027
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and 2-oxoglutarate
0.00027
purified recombinant enzyme, substrates (R)-alpha-methylbenzylamine and 2-oxoglutarate, pH and temperature not specified in the publication
0.00042
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and pyruvate
0.00042
purified recombinant enzyme, substrates (R)-alpha-methylbenzylamine and pyruvate, pH and temperature not specified in the publication
0.0014
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates L-leucine and 2-oxoglutarate
0.0014
purified recombinant enzyme, substrates L-leucine and 2-oxoglutarate, pH and temperature not specified in the publication
0.0015
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates L-leucine and 2-oxoglutarate
0.0015
purified recombinant enzyme, substrates L-leucine and 2-oxoglutarate, pH and temperature not specified in the publication
0.003
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates D-alanine and 2-oxoglutarate
0.003
purified recombinant enzyme, substrates D-alanine and 2-oxoglutarate, pH and temperature not specified in the publication
0.0042
purified enzyme, pH 10.0, 40°C, substrate 2-oxoglutarate
0.0042
purified recombinant enzyme, pH 10.0, 40°C, substrate (R)-alpha-methylbenzylamine and 2-oxoglutarate
0.007
purified enzyme, pH 10.0, 40°C, substrate pyruvate
0.007
purified recombinant enzyme, pH 10.0, 40°C, substrate (R)-alpha-methylbenzylamine and pyruvate
0.007
purified recombinant enzyme, pH 8.0, 40°C, substrates (R)-1-phenylethylamine and 3-methyl-3-oxovalerate
0.025
purified enzyme, pH 10.0, 40°C, substrate 2-oxobutyrate
0.025
purified recombinant enzyme, pH 10.0, 40°C, substrate (R)-alpha-methylbenzylamine and 2-oxobutyrate
0.046
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and 2-oxoglutarate
0.046
purified recombinant enzyme, substrates (R)-alpha-methylbenzylamine and 2-oxoglutarate, pH and temperature not specified in the publication
0.09
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and pyruvate
0.09
purified recombinant enzyme, substrates (R)-alpha-methylbenzylamine and pyruvate, pH and temperature not specified in the publication
0.12
purified enzyme, pH 10.0, 40°C, substrate 3-methyl-2-oxobutyrate
0.12
purified recombinant enzyme, pH 10.0, 40°C, substrate (R)-alpha-methylbenzylamine and 3-methyl-2-oxobutyrate
0.135
purified enzyme, pH 10.0, 40°C, substrate 2-oxohexanoate
0.135
purified recombinant enzyme, pH 10.0, 40°C, substrate (R)-alpha-methylbenzylamine and 2-oxohexanoate
0.15
purified enzyme, pH 10.0, 40°C, substrate 4-methyl-2-oxovalerate
0.15
purified recombinant enzyme, pH 10.0, 40°C, substrate (R)-alpha-methylbenzylamine and 4-methyl-2-oxovalerate
0.19
purified enzyme, pH 10.0, 40°C, substrate 3-methyl-2-oxovalerate
0.19
purified recombinant enzyme, pH 10.0, 40°C, substrate (R)-alpha-methylbenzylamine and 3-methyl-2-oxovalerate
0.23
purified enzyme, pH 10.0, 40°C, substrate 2-oxovalerate
0.23
purified recombinant enzyme, pH 10.0, 40°C, substrate (R)-alpha-methylbenzylamine and 2-oxovalerate
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physiological function
enzyme Hoch3033 is a transaminases with mixed type of activity. The mixed type of activity of Hoch3033 is implemented within the BCAT-like active site, but in the active site of Hoch3033, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes (H106Y/Y108R) result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine
evolution
(R)-selective omega-aminotransferases (R-omegaATs) are variants of aminotransferase group III
evolution
(R)-selective omega-aminotransferases (R-omegaATs) are variants of aminotransferase group III
evolution
(R)-selective omega-aminotransferases (R-omegaATs) are variants of aminotransferase group III
evolution
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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 PLP fold type IV transaminases
evolution
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases
evolution
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
evolution
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
evolution
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
evolution
the enzyme is a PLP fold type IV transaminase. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. Enzyme Hoch3033 is a transaminases with mixed type of activity. The mixed type of activity of Hoch3033 is implemented within the BCAT-like active site, but in the active site of Hoch3033, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed
evolution
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the enzyme is a PLP fold type IV transaminase. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. A small substrate binding pocket which is a general property for all the omega-TAs known to date
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
(R)-selective omega-aminotransferases (R-omegaATs) are variants of aminotransferase group III
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
(R)-selective omega-aminotransferases (R-omegaATs) are variants of aminotransferase group III
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
(R)-selective omega-aminotransferases (R-omegaATs) are variants of aminotransferase group III
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
(R)-selective omega-aminotransferases (R-omegaATs) are variants of aminotransferase group III
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
(R)-selective omega-aminotransferases (R-omegaATs) are variants of aminotransferase group III
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
additional information
-
enzyme Hoch3033 active site structure and substrate binding. Hoch3033 has changes in the specificity determining key residues, which constitute characteristic sequence motifs, overview
additional information
enzyme Hoch3033 active site structure and substrate binding. Hoch3033 has changes in the specificity determining key residues, which constitute characteristic sequence motifs, overview
additional information
-
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active structure analysis
additional information
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active structure analysis
additional information
-
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active structure analysis
-
additional information
-
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active structure analysis
-
additional information
-
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active structure analysis
-
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