Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-Oxohexanoate | inhibition of transamination by the oxo substrate at below 10 mM | Escherichia coli | |
4,4-dimethyl-2-oxovalerate | inhibition of transamination by the oxo substrate at below 10 mM | Escherichia coli | |
4-methyl-2-oxovalerate | inhibition of transamination by the oxo substrate at below 10 mM | Escherichia coli | |
L-glutamate | inhibition of transamination by the oxo substrate at above 200 mM | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.085 | - |
2-oxoglutarate | pH 8.0, 37°C | Helicobacter pylori | |
0.21 | - |
L-leucine | pH 8.0, 65°C | Thermoproteus uzoniensis | |
0.25 | - |
L-leucine | pH 8.0, 37°C | Brevibacillus brevis | |
0.3 | - |
2-oxoglutarate | pH 8.0, 30°C | Pseudomonas sp. | |
0.3 | - |
L-leucine | pH 8.0, 30°C | Pseudomonas sp. | |
0.34 | - |
L-isoleucine | pH 8.0, 37°C | Helicobacter pylori | |
0.4 | - |
2-oxoglutarate | pH 8.0, 37°C | Pseudomonas aeruginosa | |
0.42 | - |
L-leucine | pH 8.0, 25°C | Escherichia coli | |
0.56 | - |
L-glutamate | pH 8.0, 37°C | Brevibacillus brevis | |
0.57 | - |
2-oxoglutarate | pH 8.0, 37°C | Brevibacillus brevis | |
0.6 | - |
2-oxoglutarate | pH 7.5, 37°C | Methanococcus aeolicus | |
1 | - |
L-leucine | pH 8.0, 37°C | Pseudomonas aeruginosa | |
1 | - |
2-oxovalerate | pH 8.0, 37°C | Pseudomonas aeruginosa | |
1.1 | - |
L-leucine | pH 7.5, 37°C | Methanococcus aeolicus | |
1.2 | - |
3-methyl-2-oxopentanoate | pH 8.0, 37°C | Pseudomonas aeruginosa | |
1.3 | - |
L-glutamate | pH 7.4, 37°C | Mycobacterium tuberculosis | |
1.82 | - |
L-leucine | pH 9.0, 37°C | Gluconobacter oxydans | |
2.6 | - |
2-oxoglutarate | pH 8.0, 25°C | Escherichia coli | |
3.2 | - |
L-glutamate | pH 8.0, 37°C | Pseudomonas sp. | |
4.57 | - |
2-oxoglutarate | pH 9.0, 37°C | Gluconobacter oxydans | |
6.02 | - |
L-leucine | pH 7.4, 37°C | Mycobacterium tuberculosis | |
6.95 | - |
2-oxoglutarate | pH 7.4, 37°C | Mycobacterium tuberculosis | |
16 | - |
2-oxoglutarate | pH 8.0, 65°C | Thermoproteus uzoniensis | |
16.7 | - |
L-glutamate | pH 9.0, 37°C | Gluconobacter oxydans | |
18 | - |
L-glutamate | pH 8.0, 37°C | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Brevibacillus brevis | A0A2Z4MEX9 | - |
- |
Escherichia coli | P0AB80 | - |
- |
Gluconobacter oxydans | Q5FTR3 | - |
- |
Gluconobacter oxydans 621H | Q5FTR3 | - |
- |
Helicobacter pylori | O26004 | - |
- |
Helicobacter pylori 26695 | O26004 | - |
- |
Helicobacter pylori ATCC 700392 | O26004 | - |
- |
Lacticaseibacillus paracasei | A0A5Q8BPF5 | - |
- |
Lactococcus lactis | - |
- |
- |
Methanococcus aeolicus | A6UWA0 | - |
- |
Methanococcus aeolicus ATCC BAA-1280 | A6UWA0 | - |
- |
Methanococcus aeolicus DSM 17508 | A6UWA0 | - |
- |
Methanococcus aeolicus Nankai-3 | A6UWA0 | - |
- |
Methanococcus aeolicus OCM 812 | A6UWA0 | - |
- |
Mycobacterium tuberculosis | P9WQ75 | - |
- |
Mycobacterium tuberculosis ATCC 25618 | P9WQ75 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WQ75 | - |
- |
Pseudomonas aeruginosa | O86428 | - |
- |
Pseudomonas aeruginosa 1C | O86428 | - |
- |
Pseudomonas aeruginosa ATCC 15692 | O86428 | - |
- |
Pseudomonas aeruginosa CIP 104116 | O86428 | - |
- |
Pseudomonas aeruginosa DSM 22644 | O86428 | - |
- |
Pseudomonas aeruginosa JCM 14847 | O86428 | - |
- |
Pseudomonas aeruginosa LMG 12228 | O86428 | - |
- |
Pseudomonas aeruginosa PRS 101 | O86428 | - |
- |
Pseudomonas sp. | - |
- |
- |
Thermococcus sp. CKU-1 | - |
- |
- |
Thermoproteus uzoniensis | F2L0W0 | - |
- |
Thermoproteus uzoniensis 768-20 | F2L0W0 | - |
- |
Vulcanisaeta moutnovskia | F0QW25 | - |
- |
Vulcanisaeta moutnovskia 768-28 | F0QW25 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Lactococcus lactis | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Pseudomonas sp. | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Mycobacterium tuberculosis | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Escherichia coli | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Thermoproteus uzoniensis | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Pseudomonas aeruginosa | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Gluconobacter oxydans | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Lacticaseibacillus paracasei | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Brevibacillus brevis | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Helicobacter pylori | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Methanococcus aeolicus | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Vulcanisaeta moutnovskia | |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview | Thermococcus sp. CKU-1 |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.5 | - |
pH 7.5, 37°C, substrate L-leucine | Methanococcus aeolicus |
1.7 | - |
pH 8.0, 65°C, substrate L-leucine | Thermoproteus uzoniensis |
1.7 | - |
pH 8.0, 65°C, substrate L-leucine | Vulcanisaeta moutnovskia |
2.5 | - |
pH 8.0, 30°C, substrate L-leucine | Pseudomonas sp. |
11.1 | - |
pH 9.0, 37°C, substrate L-isoleucine | Lacticaseibacillus paracasei |
12.8 | - |
pH 7.4, 37°C, substrate L-leucine | Mycobacterium tuberculosis |
23.9 | - |
pH 8.0, 25°C, substrate L-leucine | Escherichia coli |
27.3 | - |
pH 8.0, 37°C, substrate L-isoleucine | Helicobacter pylori |
41.8 | - |
pH 8.0, 37°C, substrate L-leucine | Brevibacillus brevis |
42.8 | - |
pH 9.0, 37°C, substrate L-leucine | Gluconobacter oxydans |
90 | - |
pH 8.0, 37°C, substrate L-leucine | Pseudomonas aeruginosa |
94 | - |
pH 9.0, 37°C, substrate L-isoleucine | Lactococcus lactis |
390 | - |
pH 7.3, 90°C, substrate L-leucine | Thermococcus sp. CKU-1 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-aminobutyrate + L-glutamate | - |
Pseudomonas sp. | 2-oxobutyrate + 2-oxoglutarate | - |
r | |
2-oxo-3-indolylpropanoate + L-leucine | - |
Vulcanisaeta moutnovskia | L-tryptophan + 4-methyl-2-oxovalerate | - |
r | |
2-oxo-3-indolylpropanoate + L-leucine | - |
Vulcanisaeta moutnovskia 768-28 | L-tryptophan + 4-methyl-2-oxovalerate | - |
r | |
2-oxobutyrate + 2-oxoglutarate | - |
Pseudomonas sp. | 2-aminobutyrate + L-glutamate | - |
r | |
2-oxobutyrate + 2-oxoglutarate | - |
Lacticaseibacillus paracasei | 2-aminobutyrate + L-glutamate | - |
r | |
2-oxobutyrate + L-glutamate | - |
Escherichia coli | 2-aminobutyrate + 2-oxoglutarate | - |
r | |
2-oxobutyrate + L-glutamate | - |
Thermoproteus uzoniensis | 2-aminobutyrate + 2-oxoglutarate | - |
r | |
2-oxobutyrate + L-glutamate | - |
Thermococcus sp. CKU-1 | 2-aminobutyrate + 2-oxoglutarate | - |
r | |
2-oxobutyrate + L-leucine | - |
Vulcanisaeta moutnovskia | 2-aminobutyrate + 4-methyl-2-oxovalerate | - |
r | |
2-oxobutyrate + L-leucine | - |
Vulcanisaeta moutnovskia 768-28 | 2-aminobutyrate + 4-methyl-2-oxovalerate | - |
r | |
2-oxohexanoate + L-glutamate | - |
Thermococcus sp. CKU-1 | L-norleucine + 2-oxoglutarate | - |
r | |
2-oxohexanoate + L-glutamate | - |
Escherichia coli | norleucine + 2-oxoglutarate | - |
r | |
2-oxohexanoate + L-glutamate | high activity | Lacticaseibacillus paracasei | norleucine + 2-oxoglutarate | - |
r | |
2-oxovalerate + L-glutamate | - |
Escherichia coli | norvaline + 2-oxoglutarate | - |
r | |
2-oxovalerate + L-glutamate | - |
Pseudomonas aeruginosa | norvaline + 2-oxoglutarate | - |
r | |
2-oxovalerate + L-glutamate | - |
Gluconobacter oxydans | norvaline + 2-oxoglutarate | - |
r | |
3-methyl-2-oxobutanoate + L-glutamate | - |
Lactococcus lactis | L-valine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxobutanoate + L-glutamate | - |
Pseudomonas sp. | L-valine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxobutanoate + L-glutamate | - |
Mycobacterium tuberculosis | L-valine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxobutanoate + L-glutamate | - |
Pseudomonas aeruginosa | L-valine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxobutanoate + L-glutamate | - |
Lacticaseibacillus paracasei | L-valine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxobutanoate + L-glutamate | - |
Thermococcus sp. CKU-1 | L-valine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxobutanoate + L-glutamate | - |
Mycobacterium tuberculosis H37Rv | L-valine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxobutanoate + L-glutamate | - |
Mycobacterium tuberculosis ATCC 25618 | L-valine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxopentanoate + L-glutamate | - |
Thermoproteus uzoniensis | L-isoleucine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxopentanoate + L-glutamate | - |
Pseudomonas aeruginosa | L-isoleucine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxopentanoate + L-glutamate | - |
Lacticaseibacillus paracasei | L-isoleucine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxopentanoate + L-glutamate | high activity | Mycobacterium tuberculosis | L-isoleucine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxopentanoate + L-glutamate | high activity | Escherichia coli | L-isoleucine + 2-oxoglutarate | - |
r | |
3-methyl-2-oxopentanoate + L-leucine | - |
Vulcanisaeta moutnovskia | L-isoleucine + 4-methyl-2-oxovalerate | - |
r | |
3-methyl-2-oxopentanoate + L-leucine | - |
Vulcanisaeta moutnovskia 768-28 | L-isoleucine + 4-methyl-2-oxovalerate | - |
r | |
4,4-dimethyl-2-oxovalerate + L-glutamate | - |
Escherichia coli | L-neopentylglycine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-glutamate | - |
Lactococcus lactis | L-leucine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-glutamate | - |
Pseudomonas sp. | L-leucine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-glutamate | - |
Mycobacterium tuberculosis | L-leucine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-glutamate | - |
Escherichia coli | L-leucine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-glutamate | - |
Thermoproteus uzoniensis | L-leucine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-glutamate | - |
Pseudomonas aeruginosa | L-leucine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-glutamate | - |
Gluconobacter oxydans | L-leucine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-glutamate | - |
Lacticaseibacillus paracasei | L-leucine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-glutamate | - |
Brevibacillus brevis | L-leucine + 2-oxoglutarate | - |
r | |
4-methyl-2-oxopentanoate + L-leucine | - |
Vulcanisaeta moutnovskia | L-leucine + 4-methyl-2-oxovalerate | - |
r | |
4-methyl-2-oxopentanoate + L-leucine | - |
Vulcanisaeta moutnovskia 768-28 | L-leucine + 4-methyl-2-oxovalerate | - |
r | |
4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
Lactococcus lactis | L-methionine + 2-oxoglutarate | - |
r | |
4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
Mycobacterium tuberculosis | L-methionine + 2-oxoglutarate | - |
r | |
beta-phenylpyruvate + L-glutamate | - |
Lactococcus lactis | L-phenylalanine + 2-oxoglutarate | - |
r | |
beta-phenylpyruvate + L-glutamate | - |
Mycobacterium tuberculosis | L-phenylalanine + 2-oxoglutarate | - |
r | |
beta-phenylpyruvate + L-glutamate | - |
Lacticaseibacillus paracasei | L-phenylalanine + 2-oxoglutarate | - |
r | |
beta-phenylpyruvate + L-glutamate | - |
Thermococcus sp. CKU-1 | L-phenylalanine + 2-oxoglutarate | - |
r | |
glycine + 2-oxoglutarate | - |
Helicobacter pylori | glyoxylate + L-glutamate | - |
r | |
L-alanine + 2-oxoglutarate | - |
Pseudomonas sp. | pyruvate + L-glutamate | - |
r | |
L-alanine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | pyruvate + L-glutamate | - |
r | |
L-alanine + 2-oxoglutarate | - |
Brevibacillus brevis | pyruvate + L-glutamate | - |
r | |
L-alanine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | pyruvate + L-glutamate | - |
r | |
L-alanine + 2-oxoglutarate | - |
Thermoproteus uzoniensis 768-20 | pyruvate + L-glutamate | - |
r | |
L-alanine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | pyruvate + L-leucine | - |
r | |
L-arginine + 2-oxoglutarate | - |
Pseudomonas sp. | 2-oxo-5-guanidinopentanoate + L-glutamate | - |
r | |
L-aspartate + 2-oxoglutarate | - |
Pseudomonas sp. | oxaloacetate + L-glutamate | - |
r | |
L-aspartate + 2-oxoglutarate | - |
Gluconobacter oxydans | oxaloacetate + L-glutamate | - |
r | |
L-aspartate + 2-oxoglutarate | - |
Helicobacter pylori | oxaloacetate + L-glutamate | - |
r | |
L-aspartate + 2-oxoglutarate | - |
Gluconobacter oxydans 621H | oxaloacetate + L-glutamate | - |
r | |
L-aspartate + 2-oxoglutarate | - |
Helicobacter pylori ATCC 700392 | oxaloacetate + L-glutamate | - |
r | |
L-aspartate + 2-oxoglutarate | - |
Helicobacter pylori 26695 | oxaloacetate + L-glutamate | - |
r | |
L-cysteine + 2-oxoglutarate | - |
Lactococcus lactis | 2-oxo-3-thiobutyrate + L-glutamate | - |
? | |
L-cysteine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | 2-oxo-3-thiobutyrate + L-glutamate | - |
r | |
L-histidine + 2-oxoglutarate | - |
Pseudomonas sp. | 2-oxo-3-imidazolpropanoate + L-glutamate | - |
r | |
L-histidine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | 2-oxo-3-imidazolpropanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Pseudomonas sp. | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Pseudomonas aeruginosa | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Gluconobacter oxydans | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Brevibacillus brevis | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Lactococcus lactis | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Mycobacterium tuberculosis | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Escherichia coli | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Lacticaseibacillus paracasei | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Helicobacter pylori | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Methanococcus aeolicus | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Pseudomonas aeruginosa ATCC 15692 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Pseudomonas aeruginosa 1C | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Pseudomonas aeruginosa PRS 101 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Methanococcus aeolicus DSM 17508 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Pseudomonas aeruginosa DSM 22644 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Pseudomonas aeruginosa CIP 104116 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Pseudomonas aeruginosa LMG 12228 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Mycobacterium tuberculosis H37Rv | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Mycobacterium tuberculosis ATCC 25618 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Pseudomonas aeruginosa JCM 14847 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Methanococcus aeolicus OCM 812 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Methanococcus aeolicus ATCC BAA-1280 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | high activity | Methanococcus aeolicus Nankai-3 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | 3-methyl-2-oxopentanoate + L-leucine | - |
r | |
L-leucine + 2-oxoglutarate | - |
Lactococcus lactis | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Escherichia coli | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Lacticaseibacillus paracasei | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Helicobacter pylori | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Pseudomonas aeruginosa | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Gluconobacter oxydans | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Brevibacillus brevis | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | highly preferred substrates | Pseudomonas sp. | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | highly preferred substrates | Methanococcus aeolicus | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Pseudomonas aeruginosa ATCC 15692 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Gluconobacter oxydans 621H | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Pseudomonas aeruginosa 1C | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Pseudomonas aeruginosa PRS 101 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | highly preferred substrates | Methanococcus aeolicus DSM 17508 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Helicobacter pylori ATCC 700392 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Pseudomonas aeruginosa DSM 22644 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Pseudomonas aeruginosa CIP 104116 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Pseudomonas aeruginosa LMG 12228 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis H37Rv | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis ATCC 25618 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Helicobacter pylori 26695 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Thermoproteus uzoniensis 768-20 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | high activity | Pseudomonas aeruginosa JCM 14847 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | highly preferred substrates | Methanococcus aeolicus OCM 812 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | highly preferred substrates | Methanococcus aeolicus ATCC BAA-1280 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | highly preferred substrates | Methanococcus aeolicus Nankai-3 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | 4-methyl-2-oxopentanoate + L-leucine | - |
r | |
L-lysine + 2-oxoglutarate | - |
Pseudomonas sp. | 2-oxo-6-aminohexanoate + L-glutamate | - |
r | |
L-lysine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | 2-oxo-6-aminohexanoate + L-leucine | - |
r | |
L-lysine + pyruvate | - |
Thermoproteus uzoniensis | 2-oxo-6-aminohexanoate + L-alanine | - |
r | |
L-methionine + 2-oxoglutarate | - |
Lactococcus lactis | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Pseudomonas sp. | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Escherichia coli | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Pseudomonas aeruginosa | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Gluconobacter oxydans | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Lacticaseibacillus paracasei | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Brevibacillus brevis | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Helicobacter pylori | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Pseudomonas aeruginosa ATCC 15692 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Gluconobacter oxydans 621H | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Pseudomonas aeruginosa 1C | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Pseudomonas aeruginosa PRS 101 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Helicobacter pylori ATCC 700392 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Pseudomonas aeruginosa DSM 22644 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Pseudomonas aeruginosa CIP 104116 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Pseudomonas aeruginosa LMG 12228 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Helicobacter pylori 26695 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Thermoproteus uzoniensis 768-20 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 2-oxoglutarate | - |
Pseudomonas aeruginosa JCM 14847 | 4-methylsulfanyl-2-oxobutanoate + L-glutamate | - |
r | |
L-methionine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | 4-methylsulfanyl-2-oxobutanoate + L-leucine | - |
r | |
L-norleucine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | 2-oxohexanoate + L-glutamate | - |
r | |
L-norleucine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | 2-oxohexanoate + L-leucine | - |
r | |
L-norvaline + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | 2-oxovalerate + L-glutamate | - |
r | |
L-norvaline + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | 2-oxovalerate + L-leucine | - |
r | |
L-ornithine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | ? + L-glutamate | - |
r | |
L-ornithine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | ? + L-leucine | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pseudomonas sp. | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Escherichia coli | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pseudomonas aeruginosa | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Gluconobacter oxydans | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Brevibacillus brevis | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Helicobacter pylori | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Methanococcus aeolicus | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pseudomonas aeruginosa ATCC 15692 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Gluconobacter oxydans 621H | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pseudomonas aeruginosa 1C | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pseudomonas aeruginosa PRS 101 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Methanococcus aeolicus DSM 17508 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Helicobacter pylori ATCC 700392 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pseudomonas aeruginosa DSM 22644 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pseudomonas aeruginosa CIP 104116 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pseudomonas aeruginosa LMG 12228 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Helicobacter pylori 26695 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Thermoproteus uzoniensis 768-20 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Pseudomonas aeruginosa JCM 14847 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Methanococcus aeolicus OCM 812 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Methanococcus aeolicus ATCC BAA-1280 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Methanococcus aeolicus Nankai-3 | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Lactococcus lactis | beta-phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | beta-phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | beta-phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | phenylpyruvate + L-leucine | - |
r | |
L-serine + 2-oxoglutarate | - |
Pseudomonas sp. | 3-hydroxy-2-oxopropanoate + L-glutamate | - |
r | |
L-threonine + 2-oxoglutarate | - |
Pseudomonas sp. | 2-oxo-3-hydroxybutyrate + L-glutamate | - |
r | |
L-threonine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | 2-oxo-3-hydroxybutyrate + L-glutamate | - |
r | |
L-threonine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | 2-oxo-3-hydroxybutyrate + L-glutamate | - |
r | |
L-threonine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | 2-oxo-3-hydroxybutyrate + L-leucine | - |
r | |
L-tryptophan + 2-oxoglutarate | - |
Pseudomonas sp. | 2-oxo-3-indolylpropanoate + L-glutamate | - |
r | |
L-tryptophan + 2-oxoglutarate | - |
Escherichia coli | 2-oxo-3-indolylpropanoate + L-glutamate | - |
r | |
L-tryptophan + 2-oxoglutarate | - |
Gluconobacter oxydans | 2-oxo-3-indolylpropanoate + L-glutamate | - |
r | |
L-tryptophan + 2-oxoglutarate | - |
Brevibacillus brevis | 2-oxo-3-indolylpropanoate + L-glutamate | - |
r | |
L-tryptophan + 2-oxoglutarate | - |
Methanococcus aeolicus | 2-oxo-3-indolylpropanoate + L-glutamate | - |
r | |
L-tryptophan + pyruvate | - |
Vulcanisaeta moutnovskia | 2-oxo-3-indolylpropanoate + L-alanine | - |
r | |
L-tryptophan + pyruvate | - |
Thermococcus sp. CKU-1 | 2-oxo-3-indolylpropanoate + L-alanine | - |
r | |
L-tyrosine + 2-oxoglutarate | - |
Escherichia coli | 4-hydroxyphenylpyruvate + L-glutamate | - |
r | |
L-tyrosine + 2-oxoglutarate | - |
Brevibacillus brevis | 4-hydroxyphenylpyruvate + L-glutamate | - |
r | |
L-tyrosine + 2-oxoglutarate | - |
Methanococcus aeolicus | 4-hydroxyphenylpyruvate + L-glutamate | - |
r | |
L-tyrosine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | 4-hydroxyphenylpyruvate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Lactococcus lactis | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Pseudomonas sp. | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Escherichia coli | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Pseudomonas aeruginosa | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Gluconobacter oxydans | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Lacticaseibacillus paracasei | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Brevibacillus brevis | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Helicobacter pylori | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Methanococcus aeolicus | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Thermococcus sp. CKU-1 | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Methanococcus aeolicus DSM 17508 | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Mycobacterium tuberculosis H37Rv | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Mycobacterium tuberculosis ATCC 25618 | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Methanococcus aeolicus OCM 812 | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Methanococcus aeolicus ATCC BAA-1280 | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Methanococcus aeolicus Nankai-3 | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
L-valine + 4-methyl-2-oxovalerate | - |
Vulcanisaeta moutnovskia | 3-methyl-2-oxobutanoate + L-leucine | - |
r | |
additional information | the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = 3-methyl-2-oxovalerate = pyruvate, and for amino acids it is L-Met > L-ornithine > L-Thr > L-Val > L-norVal > L-His > L-Ile = L-Leu = L-norLeu > L-Phe > L-Ala > L-Lys | Thermoproteus uzoniensis | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = indole-3-pyruvate (L-Trp) > 3-methyl-2-oxovalerate > pyruvate, and for amino acids it is L-Met > L-ornithine > L-Lys > L-Thr > L-Val > L-norVal > L-Ile > L-Leu > L-norLeu > L-Ala > L-Phe > L-Trp | Vulcanisaeta moutnovskia | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 2-oxoglutarate > 3-methyl-2-oxobutanoate > 2-oxobutyrate > pyruvate, and for amino acids it is L-Leu >> L-Met > L-Val > L-2-aminobutyrate > L-Thr > L-Phe = L-Ile » L-Ala > L-Arg > L-Trp > L-Asp > L-Ser > L-His > L-Lys | Pseudomonas sp. | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 2-oxoglutarate > 4-methyl-2-oxovalerate > 2-oxoisovalerate > 4-methylthio-2-oxobutyrate (Met) > beta-phenylpyruvate (Phe) >> pyruvate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met > L-Cys > L-Phe | Lactococcus lactis | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 2-oxohexanoate > 2-oxoisovalerate > 2-oxoglutarate > 4-methylthio-2-oxobutyrate > 2-oxobutyrate = 3-methyl-2-oxovalerate = beta-phenylpyruvate >> pyruvate, and for amino acids it is L-Ile > L-Leu = L-Val >> L-Met | Lacticaseibacillus paracasei | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate (Ile) > 4-methyl-2-oxovalerate (Leu) > 4,4-dimethyl-2-oxovalerate (L-neopentylGly) > 2-oxohexanoate (norLeu) > 3-methyl-2-oxobutanoate (Val) > 2-oxovalerate (norVal) > trimethylpyruvate (L-tert-Leu) > 2-oxobutyrate > pyruvate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Phe > L-Met > L-Tyr > L-Trp | Escherichia coli | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate > 4-methyl-2-oxovalerate > 2-oxoisovalerate >> beta-phenylpyruvate > 4-methylthio-2-oxobutyrate, and for amino acids it is L-Ile = L-Leu = L-Val > L-Phe | Mycobacterium tuberculosis | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is beta-phenylpyruvate > 2-oxobutyrate > 2-oxohexanoate > 2-oxoisovalerate > 4-methyl-2-oxovalerate > 2-oxoglutarate > 2-oxovalerate, and for amino acids it is L-Leu = L-Phe > L-Met > L-norLeu > L-Val > L-norVal > L-Ile > L-2-aminobutyrate >> L-Ala = L-Trp > L-Cys > L-Tyr > L-Thr | Thermococcus sp. CKU-1 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met = L-Asp = L-Phe > L-Gly | Helicobacter pylori | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-norVal = L-norLeu = L-Val > L-Phe > L-Trp > L-Ile > L-Met >> L-Tyr >> L-Ala | Brevibacillus brevis | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe | Methanococcus aeolicus | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norLeu > L-norVal > L-Met > L-Phe > L-Asp > L-Trp | Gluconobacter oxydans | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine | Pseudomonas aeruginosa | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine | Pseudomonas aeruginosa ATCC 15692 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norLeu > L-norVal > L-Met > L-Phe > L-Asp > L-Trp | Gluconobacter oxydans 621H | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine | Pseudomonas aeruginosa 1C | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine | Pseudomonas aeruginosa PRS 101 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe | Methanococcus aeolicus DSM 17508 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met = L-Asp = L-Phe > L-Gly | Helicobacter pylori ATCC 700392 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine | Pseudomonas aeruginosa DSM 22644 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine | Pseudomonas aeruginosa CIP 104116 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine | Pseudomonas aeruginosa LMG 12228 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate > 4-methyl-2-oxovalerate > 2-oxoisovalerate >> beta-phenylpyruvate > 4-methylthio-2-oxobutyrate, and for amino acids it is L-Ile = L-Leu = L-Val > L-Phe | Mycobacterium tuberculosis H37Rv | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate > 4-methyl-2-oxovalerate > 2-oxoisovalerate >> beta-phenylpyruvate > 4-methylthio-2-oxobutyrate, and for amino acids it is L-Ile = L-Leu = L-Val > L-Phe | Mycobacterium tuberculosis ATCC 25618 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met = L-Asp = L-Phe > L-Gly | Helicobacter pylori 26695 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = indole-3-pyruvate (L-Trp) > 3-methyl-2-oxovalerate > pyruvate, and for amino acids it is L-Met > L-ornithine > L-Lys > L-Thr > L-Val > L-norVal > L-Ile > L-Leu > L-norLeu > L-Ala > L-Phe > L-Trp | Vulcanisaeta moutnovskia 768-28 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = 3-methyl-2-oxovalerate = pyruvate, and for amino acids it is L-Met > L-ornithine > L-Thr > L-Val > L-norVal > L-His > L-Ile = L-Leu = L-norLeu > L-Phe > L-Ala > L-Lys | Thermoproteus uzoniensis 768-20 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine | Pseudomonas aeruginosa JCM 14847 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe | Methanococcus aeolicus OCM 812 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe | Methanococcus aeolicus ATCC BAA-1280 | ? | - |
- |
|
additional information | the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe | Methanococcus aeolicus Nankai-3 | ? | - |
- |
|
norleucine + 2-oxoglutarate | - |
Thermoproteus uzoniensis | 2-oxohexanoate + L-glutamate | - |
r | |
norleucine + 2-oxoglutarate | - |
Gluconobacter oxydans | 2-oxohexanoate + L-glutamate | - |
r | |
norleucine + 2-oxoglutarate | - |
Brevibacillus brevis | 2-oxohexanoate + L-glutamate | - |
r | |
norvaline + 2-oxoglutarate | - |
Thermoproteus uzoniensis | 2-oxovalerate + L-glutamate | - |
r | |
norvaline + 2-oxoglutarate | - |
Pseudomonas aeruginosa | 2-oxovalerate + L-glutamate | - |
r | |
norvaline + 2-oxoglutarate | - |
Gluconobacter oxydans | 2-oxovalerate + L-glutamate | - |
r | |
norvaline + 2-oxoglutarate | - |
Brevibacillus brevis | 2-oxovalerate + L-glutamate | - |
r | |
pyruvate + L-alanine | - |
Thermoproteus uzoniensis | L-alanine + pyruvate | - |
r | |
pyruvate + L-alanine | - |
Vulcanisaeta moutnovskia | L-alanine + pyruvate | - |
r | |
pyruvate + L-glutamate | - |
Pseudomonas sp. | L-alanine + 2-oxoglutarate | - |
r | |
pyruvate + L-glutamate | low activity | Lactococcus lactis | L-alanine + 2-oxoglutarate | - |
r | |
pyruvate + L-glutamate | low activity | Lacticaseibacillus paracasei | L-alanine + 2-oxoglutarate | - |
r | |
trimethylpyruvate + L-glutamate | - |
Escherichia coli | L-tert-Leu + 2-oxoglutarate | - |
r |
Subunits | Comment | Organism |
---|---|---|
? | x * 37800, SDS-PAGE | Lacticaseibacillus paracasei |
homodimer | 2 * 34000, SDS-PAGE | Mycobacterium tuberculosis |
homodimer | 2 * 39000, SDS-PAGE | Gluconobacter oxydans |
homodimer | 2 * 47500, SDS-PAGE | Thermococcus sp. CKU-1 |
homodimer | 2 * 37400, SDS-PAGE | Lactococcus lactis |
homodimer | 2 * 37500, SDS-PAGE | Helicobacter pylori |
homodimer | 2 * 32800, SDS-PAGE | Thermoproteus uzoniensis |
homodimer | 2 * 40100, SDS-PAGE | Brevibacillus brevis |
homohexamer | 6 * 34000, SDS-PAGE | Escherichia coli |
homohexamer | 6 * 31800, SDS-PAGE | Methanococcus aeolicus |
homotetramer | 4 * 34000, SDS-PAGE | Pseudomonas aeruginosa |
homotetramer | 4 * 35300, SDS-PAGE | Vulcanisaeta moutnovskia |
Synonyms | Comment | Organism |
---|---|---|
BcaT | - |
Lactococcus lactis |
BcaT | - |
Pseudomonas sp. |
BcaT | - |
Mycobacterium tuberculosis |
BcaT | - |
Escherichia coli |
BcaT | - |
Thermoproteus uzoniensis |
BcaT | - |
Pseudomonas aeruginosa |
BcaT | - |
Gluconobacter oxydans |
BcaT | - |
Lacticaseibacillus paracasei |
BcaT | - |
Brevibacillus brevis |
BcaT | - |
Helicobacter pylori |
BcaT | - |
Methanococcus aeolicus |
BcaT | - |
Vulcanisaeta moutnovskia |
BcaT | - |
Thermococcus sp. CKU-1 |
branched-chain amino acid aminotransferase | - |
Lactococcus lactis |
branched-chain amino acid aminotransferase | - |
Pseudomonas sp. |
branched-chain amino acid aminotransferase | - |
Mycobacterium tuberculosis |
branched-chain amino acid aminotransferase | - |
Escherichia coli |
branched-chain amino acid aminotransferase | - |
Thermoproteus uzoniensis |
branched-chain amino acid aminotransferase | - |
Pseudomonas aeruginosa |
branched-chain amino acid aminotransferase | - |
Gluconobacter oxydans |
branched-chain amino acid aminotransferase | - |
Lacticaseibacillus paracasei |
branched-chain amino acid aminotransferase | - |
Brevibacillus brevis |
branched-chain amino acid aminotransferase | - |
Helicobacter pylori |
branched-chain amino acid aminotransferase | - |
Methanococcus aeolicus |
branched-chain amino acid aminotransferase | - |
Vulcanisaeta moutnovskia |
branched-chain amino acid aminotransferase | - |
Thermococcus sp. CKU-1 |
eBCAT | - |
Escherichia coli |
IlvE | - |
Helicobacter pylori |
IlvE | - |
Lactococcus lactis |
IlvE | - |
Mycobacterium tuberculosis |
IlvE | - |
Escherichia coli |
IlvE | - |
Thermoproteus uzoniensis |
IlvE | - |
Pseudomonas aeruginosa |
IlvE | - |
Gluconobacter oxydans |
IlvE | - |
Lacticaseibacillus paracasei |
IlvE | - |
Methanococcus aeolicus |
IlvE | - |
Vulcanisaeta moutnovskia |
IlvE | - |
Thermococcus sp. CKU-1 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
30 | - |
assay at | Pseudomonas sp. |
37 | - |
assay at | Lactococcus lactis |
37 | - |
assay at | Mycobacterium tuberculosis |
37 | - |
assay at | Pseudomonas aeruginosa |
37 | - |
assay at | Gluconobacter oxydans |
37 | - |
assay at | Lacticaseibacillus paracasei |
37 | - |
assay at | Brevibacillus brevis |
37 | - |
assay at | Helicobacter pylori |
37 | - |
assay at | Methanococcus aeolicus |
65 | - |
assay at | Thermoproteus uzoniensis |
65 | - |
assay at | Vulcanisaeta moutnovskia |
90 | - |
assay at | Thermococcus sp. CKU-1 |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.07 | - |
3-methyl-2-oxopentanoate | pH 8.0, 25°C | Escherichia coli | |
0.08 | - |
4-methyl-2-oxopentanoate | pH 8.0, 25°C | Escherichia coli | |
0.08 | - |
4,4-dimethyl-2-oxovalerate | pH 8.0, 25°C | Escherichia coli | |
0.15 | - |
trimethylpyruvate | pH 8.0, 25°C | Escherichia coli | |
0.2 | - |
3-methyl-2-oxobutanoate | pH 8.0, 25°C | Escherichia coli | |
0.22 | - |
2-Oxohexanoate | pH 8.0, 25°C | Escherichia coli | |
0.6 | - |
2-oxovalerate | pH 8.0, 25°C | Escherichia coli | |
3.37 | - |
2-oxobutyrate | pH 8.0, 25°C | Escherichia coli | |
48 | - |
L-leucine | pH 8.0, 25°C | Escherichia coli | |
48 | - |
L-isoleucine | pH 8.0, 25°C | Escherichia coli | |
56 | - |
pyruvate | pH 8.0, 25°C | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.3 | - |
assay at | Thermococcus sp. CKU-1 |
7.4 | - |
assay at | Mycobacterium tuberculosis |
7.4 | - |
assay at | Lacticaseibacillus paracasei |
7.5 | - |
assay at | Lactococcus lactis |
7.5 | - |
assay at | Methanococcus aeolicus |
8 | - |
assay at | Pseudomonas sp. |
8 | - |
assay at | Escherichia coli |
8 | - |
assay at | Thermoproteus uzoniensis |
8 | - |
assay at | Pseudomonas aeruginosa |
8 | - |
assay at | Brevibacillus brevis |
8 | - |
assay at | Helicobacter pylori |
8 | - |
assay at | Vulcanisaeta moutnovskia |
9 | - |
assay at | Gluconobacter oxydans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | PLP, dependent on | Lactococcus lactis | |
pyridoxal 5'-phosphate | PLP, dependent on | Pseudomonas sp. | |
pyridoxal 5'-phosphate | PLP, dependent on | Mycobacterium tuberculosis | |
pyridoxal 5'-phosphate | PLP, dependent on | Escherichia coli | |
pyridoxal 5'-phosphate | PLP, dependent on | Thermoproteus uzoniensis | |
pyridoxal 5'-phosphate | PLP, dependent on | Pseudomonas aeruginosa | |
pyridoxal 5'-phosphate | PLP, dependent on | Gluconobacter oxydans | |
pyridoxal 5'-phosphate | PLP, dependent on | Lacticaseibacillus paracasei | |
pyridoxal 5'-phosphate | PLP, dependent on | Brevibacillus brevis | |
pyridoxal 5'-phosphate | PLP, dependent on | Helicobacter pylori | |
pyridoxal 5'-phosphate | PLP, dependent on | Methanococcus aeolicus | |
pyridoxal 5'-phosphate | PLP, dependent on | Vulcanisaeta moutnovskia | |
pyridoxal 5'-phosphate | PLP, dependent on | Thermococcus sp. CKU-1 |
General Information | Comment | Organism |
---|---|---|
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Lactococcus lactis |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Pseudomonas sp. |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Mycobacterium tuberculosis |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Escherichia coli |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Thermoproteus uzoniensis |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Pseudomonas aeruginosa |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Gluconobacter oxydans |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Lacticaseibacillus paracasei |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Brevibacillus brevis |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Helicobacter pylori |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Methanococcus aeolicus |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Vulcanisaeta moutnovskia |
evolution | branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis | Thermococcus sp. CKU-1 |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Lactococcus lactis |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Pseudomonas sp. |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Mycobacterium tuberculosis |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Escherichia coli |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Thermoproteus uzoniensis |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Pseudomonas aeruginosa |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Gluconobacter oxydans |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Lacticaseibacillus paracasei |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Brevibacillus brevis |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Helicobacter pylori |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Methanococcus aeolicus |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Vulcanisaeta moutnovskia |
metabolism | BCAT are the key enzymes of BCAA metabolism in all organisms | Thermococcus sp. CKU-1 |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Lactococcus lactis |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Pseudomonas sp. |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Mycobacterium tuberculosis |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Escherichia coli |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Thermoproteus uzoniensis |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Pseudomonas aeruginosa |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Gluconobacter oxydans |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Lacticaseibacillus paracasei |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Brevibacillus brevis |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Helicobacter pylori |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Methanococcus aeolicus |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Vulcanisaeta moutnovskia |
additional information | structure-function analysis and substrate specificity, comparisons, overview | Thermococcus sp. CKU-1 |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Lactococcus lactis |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Pseudomonas sp. |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Mycobacterium tuberculosis |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Escherichia coli |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Thermoproteus uzoniensis |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Pseudomonas aeruginosa |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Gluconobacter oxydans |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Lacticaseibacillus paracasei |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Brevibacillus brevis |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Helicobacter pylori |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Methanococcus aeolicus |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Vulcanisaeta moutnovskia |
physiological function | branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP) | Thermococcus sp. CKU-1 |