Cloned (Comment) | Organism |
---|---|
gene aat, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli | Pediococcus acidilactici |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-aminobutanoate + 2-oxoglutarate | Pediococcus acidilactici | - |
succinate semialdehyde + L-glutamate | - |
? | |
2-aminobutanoate + 2-oxoglutarate | Pediococcus acidilactici FAM18098 | - |
succinate semialdehyde + L-glutamate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pediococcus acidilactici | - |
- |
- |
Pediococcus acidilactici FAM18098 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography | Pediococcus acidilactici |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-aminobutanoate + 2-oxobutyrate | high activity in the reverse reaction | Pediococcus acidilactici | succinate semialdehyde + ? | - |
r | |
2-aminobutanoate + 2-oxoglutarate | - |
Pediococcus acidilactici | succinate semialdehyde + L-glutamate | - |
? | |
2-aminobutanoate + 2-oxoglutarate | high activity | Pediococcus acidilactici | succinate semialdehyde + L-glutamate | - |
r | |
2-aminobutanoate + 2-oxoglutarate | - |
Pediococcus acidilactici FAM18098 | succinate semialdehyde + L-glutamate | - |
? | |
L-alanine + 2-oxoglutarate | - |
Pediococcus acidilactici | pyruvate + L-glutamate | - |
r | |
L-alanine + 2-oxoglutarate | - |
Pediococcus acidilactici FAM18098 | pyruvate + L-glutamate | - |
r | |
L-cysteine + 2-oxoglutarate | - |
Pediococcus acidilactici | mercaptopyruvate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | best substrate | Pediococcus acidilactici | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | best substrate | Pediococcus acidilactici FAM18098 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | high activity | Pediococcus acidilactici | 4-(methylsulfanyl)-2-oxobutanoate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pediococcus acidilactici | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pediococcus acidilactici FAM18098 | phenylpyruvate + L-glutamate | - |
r | |
additional information | substrate specificity, overview. The transaminase catalyzes the reversible transfer of the amino group from L-Leu, L-Met, 2-aminobutanoate (AABA), L-Ala, L-Cys, and L-Phe to the amino group acceptor 2-oxoglutarate. 2-Oxobutyrate can replace 2-oxoglutarate as an amino group acceptor. In this case, AABA is produced at significantly higher levels than glutamate. No activity with L-Ser, L-Asp, L-Ile, L-Val, and L-Thr | Pediococcus acidilactici | ? | - |
- |
|
additional information | substrate specificity, overview. The transaminase catalyzes the reversible transfer of the amino group from L-Leu, L-Met, 2-aminobutanoate (AABA), L-Ala, L-Cys, and L-Phe to the amino group acceptor 2-oxoglutarate. 2-Oxobutyrate can replace 2-oxoglutarate as an amino group acceptor. In this case, AABA is produced at significantly higher levels than glutamate. No activity with L-Ser, L-Asp, L-Ile, L-Val, and L-Thr | Pediococcus acidilactici FAM18098 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
AAT | - |
Pediococcus acidilactici |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Pediococcus acidilactici |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
assay at | Pediococcus acidilactici |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Pediococcus acidilactici |
General Information | Comment | Organism |
---|---|---|
physiological function | Pediococcus acidilactici possesses a species-specific aminotransferase. The aminotransferase catalyzes the reversible transfer of an amino group to 2-oxo butyrate to form 2-aminobutyrate. The aminotransferase uses a variety of amino acids as amino group donor. During cheese ripening, the bacterial Pediococcus acidilactici strains all produce the non-proteinogenic amino acid, alpha-aminobutyrate (AABA) | Pediococcus acidilactici |