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Literature summary for 2.6.1.42 extracted from
- Identification of (R)-selective omega-aminotransferases by exploring evolutionary sequence space (2018), Enzyme Microb. Technol., 110, 46-52 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ilvE, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Evansella cellulosilytica |
| gene ilvE1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus thuringiensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus thuringiensis | A0A1B1L2T7 | serovar berliner ATCC 10792 | - |
| Evansella cellulosilytica | E6TUA8 | - |
- |
| Evansella cellulosilytica ATCC 21833 | E6TUA8 | - |
- |
| Evansella cellulosilytica DSM 2522 | E6TUA8 | - |
- |
| Evansella cellulosilytica FERM P-1141 | E6TUA8 | - |
- |
| Evansella cellulosilytica JCM 9156 | E6TUA8 | - |
- |
| Evansella cellulosilytica N-4 | E6TUA8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration | Evansella cellulosilytica |
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration | Bacillus thuringiensis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.000087 | - |
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and 2-oxoglutarate | Bacillus thuringiensis |
| 0.00022 | - |
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and pyruvate | Bacillus thuringiensis |
| 0.00027 | - |
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and 2-oxoglutarate | Evansella cellulosilytica |
| 0.00042 | - |
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates (R)-alpha-methylbenzylamine and pyruvate | Evansella cellulosilytica |
| 0.0014 | - |
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates L-leucine and 2-oxoglutarate | Evansella cellulosilytica |
| 0.0015 | - |
purified recombinant enzyme, pH 7.0, temperature not specified in the publication, substrates L-leucine and 2-oxoglutarate | Bacillus thuringiensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (R)-alpha-methylbenzylamine + 2-oxoglutarate | very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica | acetophenone + D-glutamate | - |
r |  |
| (R)-alpha-methylbenzylamine + 2-oxoglutarate | very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Bacillus thuringiensis | acetophenone + D-glutamate | - |
r | |
| (R)-alpha-methylbenzylamine + 2-oxoglutarate | very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica FERM P-1141 | acetophenone + D-glutamate | - |
r | |
| (R)-alpha-methylbenzylamine + 2-oxoglutarate | very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica ATCC 21833 | acetophenone + D-glutamate | - |
r | |
| (R)-alpha-methylbenzylamine + 2-oxoglutarate | very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica DSM 2522 | acetophenone + D-glutamate | - |
r | |
| (R)-alpha-methylbenzylamine + 2-oxoglutarate | very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica JCM 9156 | acetophenone + D-glutamate | - |
r | |
| (R)-alpha-methylbenzylamine + 2-oxoglutarate | very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica N-4 | acetophenone + D-glutamate | - |
r | |
| (R)-alpha-methylbenzylamine + pyruvate | the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica | acetophenone + D-alanine | - |
r | |
| (R)-alpha-methylbenzylamine + pyruvate | the enzyme prefers pyruvate as the amino acceptor, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Bacillus thuringiensis | acetophenone + D-alanine | - |
r | |
| (R)-alpha-methylbenzylamine + pyruvate | the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica FERM P-1141 | acetophenone + D-alanine | - |
r | |
| (R)-alpha-methylbenzylamine + pyruvate | the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica ATCC 21833 | acetophenone + D-alanine | - |
r | |
| (R)-alpha-methylbenzylamine + pyruvate | the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica DSM 2522 | acetophenone + D-alanine | - |
r | |
| (R)-alpha-methylbenzylamine + pyruvate | the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica JCM 9156 | acetophenone + D-alanine | - |
r | |
| (R)-alpha-methylbenzylamine + pyruvate | the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1. | Evansella cellulosilytica N-4 | acetophenone + D-alanine | - |
r | |
| L-leucine + 2-oxoglutarate | - |
Evansella cellulosilytica | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
| L-leucine + 2-oxoglutarate | - |
Bacillus thuringiensis | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
| L-leucine + 2-oxoglutarate | - |
Evansella cellulosilytica FERM P-1141 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
| L-leucine + 2-oxoglutarate | - |
Evansella cellulosilytica ATCC 21833 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
| L-leucine + 2-oxoglutarate | - |
Evansella cellulosilytica DSM 2522 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
| L-leucine + 2-oxoglutarate | - |
Evansella cellulosilytica JCM 9156 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
| L-leucine + 2-oxoglutarate | - |
Evansella cellulosilytica N-4 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
| 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 low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity | Evansella cellulosilytica | ? | - |
- |
|
| 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 low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity | Bacillus thuringiensis | ? | - |
- |
|
| 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 low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity | Evansella cellulosilytica FERM P-1141 | ? | - |
- |
|
| 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 low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity | Evansella cellulosilytica ATCC 21833 | ? | - |
- |
|
| 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 low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity | Evansella cellulosilytica DSM 2522 | ? | - |
- |
|
| 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 low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity | Evansella cellulosilytica JCM 9156 | ? | - |
- |
|
| 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 low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity | Evansella cellulosilytica N-4 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| (R)-selective omega-aminotransferase | - |
Evansella cellulosilytica |
| (R)-selective omega-aminotransferase | - |
Bacillus thuringiensis |
| IlvE | - |
Evansella cellulosilytica |
| ilvE1 | - |
Bacillus thuringiensis |
| More | see also EC 2.6.1. | Evansella cellulosilytica |
| More | see also EC 2.6.1. | Bacillus thuringiensis |
| R-omegaAT | - |
Evansella cellulosilytica |
| R-omegaAT | - |
Bacillus thuringiensis |
| R-omegaAT_Bcel | - |
Evansella cellulosilytica |
| R-omegaAT_Bthu | - |
Bacillus thuringiensis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Evansella cellulosilytica |
| 7 | - |
assay at | Bacillus thuringiensis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | PLP, dependent on | Evansella cellulosilytica | |
| pyridoxal 5'-phosphate | PLP, dependent on | Bacillus thuringiensis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Evansella cellulosilytica |
| 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 | Bacillus thuringiensis |
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