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Literature summary extracted from

  • Bezsudnova, E.Y.; Boyko, K.M.; Popov, V.O.
    Properties of bacterial and archaeal branched-chain amino acid aminotransferases (2017), Biochemistry (Moscow), 82, 1572-1591.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.42 2-Oxohexanoate inhibition of transamination by the oxo substrate at below 10 mM Escherichia coli
2.6.1.42 4,4-dimethyl-2-oxovalerate inhibition of transamination by the oxo substrate at below 10 mM Escherichia coli
2.6.1.42 4-methyl-2-oxovalerate inhibition of transamination by the oxo substrate at below 10 mM Escherichia coli
2.6.1.42 L-glutamate inhibition of transamination by the oxo substrate at above 200 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.42 0.085
-
 2-oxoglutarate pH 8.0, 37°C Helicobacter pylori
2.6.1.42 0.21
-
 L-leucine pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 0.25
-
 L-leucine pH 8.0, 37°C Brevibacillus brevis
2.6.1.42 0.3
-
 L-leucine pH 8.0, 30°C Pseudomonas sp.
2.6.1.42 0.3
-
 2-oxoglutarate pH 8.0, 30°C Pseudomonas sp.
2.6.1.42 0.34
-
 L-isoleucine pH 8.0, 37°C Helicobacter pylori
2.6.1.42 0.4
-
 2-oxoglutarate pH 8.0, 37°C Pseudomonas aeruginosa
2.6.1.42 0.42
-
 L-leucine pH 8.0, 25°C Escherichia coli
2.6.1.42 0.56
-
 L-glutamate pH 8.0, 37°C Brevibacillus brevis
2.6.1.42 0.57
-
 2-oxoglutarate pH 8.0, 37°C Brevibacillus brevis
2.6.1.42 0.6
-
 2-oxoglutarate pH 7.5, 37°C Methanococcus aeolicus
2.6.1.42 1
-
 L-leucine pH 8.0, 37°C Pseudomonas aeruginosa
2.6.1.42 1
-
 2-oxovalerate pH 8.0, 37°C Pseudomonas aeruginosa
2.6.1.42 1.1
-
 L-leucine pH 7.5, 37°C Methanococcus aeolicus
2.6.1.42 1.2
-
 3-methyl-2-oxopentanoate pH 8.0, 37°C Pseudomonas aeruginosa
2.6.1.42 1.3
-
 L-glutamate pH 7.4, 37°C Mycobacterium tuberculosis
2.6.1.42 1.82
-
 L-leucine pH 9.0, 37°C Gluconobacter oxydans
2.6.1.42 2.6
-
 2-oxoglutarate pH 8.0, 25°C Escherichia coli
2.6.1.42 3.2
-
 L-glutamate pH 8.0, 37°C Pseudomonas sp.
2.6.1.42 4.57
-
 2-oxoglutarate pH 9.0, 37°C Gluconobacter oxydans
2.6.1.42 6.02
-
 L-leucine pH 7.4, 37°C Mycobacterium tuberculosis
2.6.1.42 6.95
-
 2-oxoglutarate pH 7.4, 37°C Mycobacterium tuberculosis
2.6.1.42 16
-
 2-oxoglutarate pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 16.7
-
 L-glutamate pH 9.0, 37°C Gluconobacter oxydans
2.6.1.42 18
-
 L-glutamate pH 8.0, 37°C Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.42 Brevibacillus brevis A0A2Z4MEX9
-
-
2.6.1.42 Escherichia coli P0AB80
-
-
2.6.1.42 Gluconobacter oxydans Q5FTR3
-
-
2.6.1.42 Gluconobacter oxydans 621H Q5FTR3
-
-
2.6.1.42 Helicobacter pylori O26004
-
-
2.6.1.42 Helicobacter pylori 26695 O26004
-
-
2.6.1.42 Helicobacter pylori ATCC 700392 O26004
-
-
2.6.1.42 Lacticaseibacillus paracasei A0A5Q8BPF5
-
-
2.6.1.42 Lactococcus lactis
-
-
-
2.6.1.42 Methanococcus aeolicus A6UWA0
-
-
2.6.1.42 Methanococcus aeolicus ATCC BAA-1280 A6UWA0
-
-
2.6.1.42 Methanococcus aeolicus DSM 17508 A6UWA0
-
-
2.6.1.42 Methanococcus aeolicus Nankai-3 A6UWA0
-
-
2.6.1.42 Methanococcus aeolicus OCM 812 A6UWA0
-
-
2.6.1.42 Mycobacterium tuberculosis P9WQ75
-
-
2.6.1.42 Mycobacterium tuberculosis ATCC 25618 P9WQ75
-
-
2.6.1.42 Mycobacterium tuberculosis H37Rv P9WQ75
-
-
2.6.1.42 Pseudomonas aeruginosa O86428
-
-
2.6.1.42 Pseudomonas aeruginosa 1C O86428
-
-
2.6.1.42 Pseudomonas aeruginosa ATCC 15692 O86428
-
-
2.6.1.42 Pseudomonas aeruginosa CIP 104116 O86428
-
-
2.6.1.42 Pseudomonas aeruginosa DSM 22644 O86428
-
-
2.6.1.42 Pseudomonas aeruginosa JCM 14847 O86428
-
-
2.6.1.42 Pseudomonas aeruginosa LMG 12228 O86428
-
-
2.6.1.42 Pseudomonas aeruginosa PRS 101 O86428
-
-
2.6.1.42 Pseudomonas sp.
-
-
-
2.6.1.42 Thermococcus sp. CKU-1
-
-
-
2.6.1.42 Thermoproteus uzoniensis F2L0W0
-
-
2.6.1.42 Thermoproteus uzoniensis 768-20 F2L0W0
-
-
2.6.1.42 Vulcanisaeta moutnovskia F0QW25
-
-
2.6.1.42 Vulcanisaeta moutnovskia 768-28 F0QW25
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.6.1.42 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
a
2.6.1.42 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
a
2.6.1.42 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.
a
2.6.1.42 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
a
2.6.1.42 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
a
2.6.1.42 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
a
2.6.1.42 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
a
2.6.1.42 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
a
2.6.1.42 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
a
2.6.1.42 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
a
2.6.1.42 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
a
2.6.1.42 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
a
2.6.1.42 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
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.42 1.5
-
 pH 7.5, 37°C, substrate L-leucine Methanococcus aeolicus
2.6.1.42 1.7
-
 pH 8.0, 65°C, substrate L-leucine Thermoproteus uzoniensis
2.6.1.42 1.7
-
 pH 8.0, 65°C, substrate L-leucine Vulcanisaeta moutnovskia
2.6.1.42 2.5
-
 pH 8.0, 30°C, substrate L-leucine Pseudomonas sp.
2.6.1.42 11.1
-
 pH 9.0, 37°C, substrate L-isoleucine Lacticaseibacillus paracasei
2.6.1.42 12.8
-
 pH 7.4, 37°C, substrate L-leucine Mycobacterium tuberculosis
2.6.1.42 23.9
-
 pH 8.0, 25°C, substrate L-leucine Escherichia coli
2.6.1.42 27.3
-
 pH 8.0, 37°C, substrate L-isoleucine Helicobacter pylori
2.6.1.42 41.8
-
 pH 8.0, 37°C, substrate L-leucine Brevibacillus brevis
2.6.1.42 42.8
-
 pH 9.0, 37°C, substrate L-leucine Gluconobacter oxydans
2.6.1.42 90
-
 pH 8.0, 37°C, substrate L-leucine Pseudomonas aeruginosa
2.6.1.42 94
-
 pH 9.0, 37°C, substrate L-isoleucine Lactococcus lactis
2.6.1.42 390
-
 pH 7.3, 90°C, substrate L-leucine Thermococcus sp. CKU-1

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.42 2-aminobutyrate + L-glutamate
-
 Pseudomonas sp. 2-oxobutyrate + 2-oxoglutarate
-
 r
2.6.1.42 2-oxo-3-indolylpropanoate + L-leucine
-
 Vulcanisaeta moutnovskia L-tryptophan + 4-methyl-2-oxovalerate
-
 r
2.6.1.42 2-oxobutyrate + 2-oxoglutarate
-
 Pseudomonas sp. 2-aminobutyrate + L-glutamate
-
 r
2.6.1.42 2-oxobutyrate + 2-oxoglutarate
-
 Lacticaseibacillus paracasei 2-aminobutyrate + L-glutamate
-
 r
2.6.1.42 2-oxobutyrate + L-glutamate
-
 Escherichia coli 2-aminobutyrate + 2-oxoglutarate
-
 r
2.6.1.42 2-oxobutyrate + L-glutamate
-
 Thermoproteus uzoniensis 2-aminobutyrate + 2-oxoglutarate
-
 r
2.6.1.42 2-oxobutyrate + L-glutamate
-
 Thermococcus sp. CKU-1 2-aminobutyrate + 2-oxoglutarate
-
 r
2.6.1.42 2-oxobutyrate + L-leucine
-
 Vulcanisaeta moutnovskia 2-aminobutyrate + 4-methyl-2-oxovalerate
-
 r
2.6.1.42 2-oxohexanoate + L-glutamate
-
 Thermococcus sp. CKU-1 L-norleucine + 2-oxoglutarate
-
 r
2.6.1.42 2-oxohexanoate + L-glutamate
-
 Escherichia coli norleucine + 2-oxoglutarate
-
 r
2.6.1.42 2-oxohexanoate + L-glutamate high activity Lacticaseibacillus paracasei norleucine + 2-oxoglutarate
-
 r
2.6.1.42 2-oxovalerate + L-glutamate
-
 Escherichia coli norvaline + 2-oxoglutarate
-
 r
2.6.1.42 2-oxovalerate + L-glutamate
-
 Pseudomonas aeruginosa norvaline + 2-oxoglutarate
-
 r
2.6.1.42 2-oxovalerate + L-glutamate
-
 Gluconobacter oxydans norvaline + 2-oxoglutarate
-
 r
2.6.1.42 2-oxovalerate + L-glutamate
-
 Gluconobacter oxydans 621H norvaline + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Pseudomonas aeruginosa L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Pseudomonas sp. L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Lactococcus lactis L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Lacticaseibacillus paracasei L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Mycobacterium tuberculosis L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Thermococcus sp. CKU-1 L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Mycobacterium tuberculosis H37Rv L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Pseudomonas aeruginosa ATCC 15692 L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Mycobacterium tuberculosis ATCC 25618 L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Pseudomonas aeruginosa DSM 22644 L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Pseudomonas aeruginosa CIP 104116 L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Pseudomonas aeruginosa JCM 14847 L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Pseudomonas aeruginosa LMG 12228 L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Pseudomonas aeruginosa 1C L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxobutanoate + L-glutamate
-
 Pseudomonas aeruginosa PRS 101 L-valine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxopentanoate + L-glutamate high activity Escherichia coli L-isoleucine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas aeruginosa L-isoleucine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxopentanoate + L-glutamate
-
 Lacticaseibacillus paracasei L-isoleucine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxopentanoate + L-glutamate high activity Mycobacterium tuberculosis L-isoleucine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxopentanoate + L-glutamate
-
 Thermoproteus uzoniensis L-isoleucine + 2-oxoglutarate
-
 r
2.6.1.42 3-methyl-2-oxopentanoate + L-leucine
-
 Vulcanisaeta moutnovskia L-isoleucine + 4-methyl-2-oxovalerate
-
 r
2.6.1.42 4,4-dimethyl-2-oxovalerate + L-glutamate
-
 Escherichia coli L-neopentylglycine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Escherichia coli L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas aeruginosa L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas sp. L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Gluconobacter oxydans L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Lactococcus lactis L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Lacticaseibacillus paracasei L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Brevibacillus brevis L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Mycobacterium tuberculosis L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Thermoproteus uzoniensis L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Mycobacterium tuberculosis H37Rv L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Gluconobacter oxydans 621H L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas aeruginosa ATCC 15692 L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Mycobacterium tuberculosis ATCC 25618 L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas aeruginosa DSM 22644 L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas aeruginosa CIP 104116 L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas aeruginosa JCM 14847 L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas aeruginosa LMG 12228 L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas aeruginosa 1C L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-glutamate
-
 Pseudomonas aeruginosa PRS 101 L-leucine + 2-oxoglutarate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-leucine
-
 Vulcanisaeta moutnovskia L-leucine + 4-methyl-2-oxovalerate
-
 r
2.6.1.42 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 Lactococcus lactis L-methionine + 2-oxoglutarate
-
 r
2.6.1.42 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 Mycobacterium tuberculosis L-methionine + 2-oxoglutarate
-
 r
2.6.1.42 beta-phenylpyruvate + L-glutamate
-
 Lactococcus lactis L-phenylalanine + 2-oxoglutarate
-
 r
2.6.1.42 beta-phenylpyruvate + L-glutamate
-
 Lacticaseibacillus paracasei L-phenylalanine + 2-oxoglutarate
-
 r
2.6.1.42 beta-phenylpyruvate + L-glutamate
-
 Mycobacterium tuberculosis L-phenylalanine + 2-oxoglutarate
-
 r
2.6.1.42 beta-phenylpyruvate + L-glutamate
-
 Thermococcus sp. CKU-1 L-phenylalanine + 2-oxoglutarate
-
 r
2.6.1.42 glycine + 2-oxoglutarate
-
 Helicobacter pylori glyoxylate + L-glutamate
-
 r
2.6.1.42 L-alanine + 2-oxoglutarate
-
 Pseudomonas sp. pyruvate + L-glutamate
-
 r
2.6.1.42 L-alanine + 2-oxoglutarate
-
 Brevibacillus brevis pyruvate + L-glutamate
-
 r
2.6.1.42 L-alanine + 2-oxoglutarate
-
 Thermoproteus uzoniensis pyruvate + L-glutamate
-
 r
2.6.1.42 L-alanine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 pyruvate + L-glutamate
-
 r
2.6.1.42 L-alanine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia pyruvate + L-leucine
-
 r
2.6.1.42 L-arginine + 2-oxoglutarate
-
 Pseudomonas sp. 2-oxo-5-guanidinopentanoate + L-glutamate
-
 r
2.6.1.42 L-aspartate + 2-oxoglutarate
-
 Pseudomonas sp. oxaloacetate + L-glutamate
-
 r
2.6.1.42 L-aspartate + 2-oxoglutarate
-
 Gluconobacter oxydans oxaloacetate + L-glutamate
-
 r
2.6.1.42 L-aspartate + 2-oxoglutarate
-
 Helicobacter pylori oxaloacetate + L-glutamate
-
 r
2.6.1.42 L-cysteine + 2-oxoglutarate
-
 Lactococcus lactis 2-oxo-3-thiobutyrate + L-glutamate
-
 ?
2.6.1.42 L-cysteine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 2-oxo-3-thiobutyrate + L-glutamate
-
 r
2.6.1.42 L-histidine + 2-oxoglutarate
-
 Pseudomonas sp. 2-oxo-3-imidazolpropanoate + L-glutamate
-
 r
2.6.1.42 L-histidine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 2-oxo-3-imidazolpropanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Escherichia coli 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Pseudomonas aeruginosa 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Pseudomonas sp. 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Gluconobacter oxydans 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Lactococcus lactis 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Lacticaseibacillus paracasei 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Brevibacillus brevis 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Helicobacter pylori 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Mycobacterium tuberculosis 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Methanococcus aeolicus 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Mycobacterium tuberculosis H37Rv 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Gluconobacter oxydans 621H 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Pseudomonas aeruginosa ATCC 15692 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Mycobacterium tuberculosis ATCC 25618 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Helicobacter pylori ATCC 700392 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Pseudomonas aeruginosa DSM 22644 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Methanococcus aeolicus DSM 17508 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Helicobacter pylori 26695 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Pseudomonas aeruginosa CIP 104116 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Pseudomonas aeruginosa JCM 14847 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Pseudomonas aeruginosa LMG 12228 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Pseudomonas aeruginosa 1C 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Pseudomonas aeruginosa PRS 101 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Methanococcus aeolicus ATCC BAA-1280 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Methanococcus aeolicus OCM 812 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate high activity Methanococcus aeolicus Nankai-3 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 3-methyl-2-oxopentanoate + L-leucine
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Escherichia coli 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Pseudomonas aeruginosa 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate highly preferred substrates Pseudomonas sp. 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Gluconobacter oxydans 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Lactococcus lactis 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Lacticaseibacillus paracasei 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Brevibacillus brevis 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Helicobacter pylori 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Mycobacterium tuberculosis 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate highly preferred substrates Methanococcus aeolicus 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Mycobacterium tuberculosis H37Rv 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Gluconobacter oxydans 621H 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Pseudomonas aeruginosa ATCC 15692 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Mycobacterium tuberculosis ATCC 25618 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Helicobacter pylori ATCC 700392 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Pseudomonas aeruginosa DSM 22644 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate highly preferred substrates Methanococcus aeolicus DSM 17508 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Helicobacter pylori 26695 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Pseudomonas aeruginosa CIP 104116 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Pseudomonas aeruginosa JCM 14847 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Pseudomonas aeruginosa LMG 12228 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Pseudomonas aeruginosa 1C 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate high activity Pseudomonas aeruginosa PRS 101 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate highly preferred substrates Methanococcus aeolicus ATCC BAA-1280 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate highly preferred substrates Methanococcus aeolicus OCM 812 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate highly preferred substrates Methanococcus aeolicus Nankai-3 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 4-methyl-2-oxopentanoate + L-leucine
-
 r
2.6.1.42 L-lysine + 2-oxoglutarate
-
 Pseudomonas sp. 2-oxo-6-aminohexanoate + L-glutamate
-
 r
2.6.1.42 L-lysine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 2-oxo-6-aminohexanoate + L-leucine
-
 r
2.6.1.42 L-lysine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 768-28 2-oxo-6-aminohexanoate + L-leucine
-
 r
2.6.1.42 L-lysine + pyruvate
-
 Thermoproteus uzoniensis 2-oxo-6-aminohexanoate + L-alanine
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Escherichia coli 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Pseudomonas aeruginosa 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Pseudomonas sp. 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Gluconobacter oxydans 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Lactococcus lactis 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Lacticaseibacillus paracasei 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Brevibacillus brevis 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Helicobacter pylori 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Helicobacter pylori ATCC 700392 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 768-20 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 2-oxoglutarate
-
 Helicobacter pylori 26695 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-methionine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 4-methylsulfanyl-2-oxobutanoate + L-leucine
-
 r
2.6.1.42 L-methionine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 768-28 4-methylsulfanyl-2-oxobutanoate + L-leucine
-
 r
2.6.1.42 L-norleucine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 2-oxohexanoate + L-glutamate
-
 r
2.6.1.42 L-norleucine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 2-oxohexanoate + L-leucine
-
 r
2.6.1.42 L-norvaline + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 2-oxovalerate + L-glutamate
-
 r
2.6.1.42 L-norvaline + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 2-oxovalerate + L-leucine
-
 r
2.6.1.42 L-ornithine + 2-oxoglutarate
-
 Thermoproteus uzoniensis ? + L-glutamate
-
 r
2.6.1.42 L-ornithine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 768-20 ? + L-glutamate
-
 r
2.6.1.42 L-ornithine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia ? + L-leucine
-
 r
2.6.1.42 L-ornithine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 768-28 ? + L-leucine
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Escherichia coli phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Pseudomonas aeruginosa phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Pseudomonas sp. phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Gluconobacter oxydans phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Brevibacillus brevis phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Helicobacter pylori phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Methanococcus aeolicus phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Thermoproteus uzoniensis phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Helicobacter pylori ATCC 700392 phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Methanococcus aeolicus DSM 17508 phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Helicobacter pylori 26695 phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Methanococcus aeolicus ATCC BAA-1280 phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Methanococcus aeolicus OCM 812 phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Methanococcus aeolicus Nankai-3 phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Lactococcus lactis beta-phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Mycobacterium tuberculosis beta-phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 beta-phenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-phenylalanine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia phenylpyruvate + L-leucine
-
 r
2.6.1.42 L-serine + 2-oxoglutarate
-
 Pseudomonas sp. 3-hydroxy-2-oxopropanoate + L-glutamate
-
 r
2.6.1.42 L-threonine + 2-oxoglutarate
-
 Pseudomonas sp. 2-oxo-3-hydroxybutyrate + L-glutamate
-
 r
2.6.1.42 L-threonine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 2-oxo-3-hydroxybutyrate + L-glutamate
-
 r
2.6.1.42 L-threonine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 2-oxo-3-hydroxybutyrate + L-glutamate
-
 r
2.6.1.42 L-threonine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 768-20 2-oxo-3-hydroxybutyrate + L-glutamate
-
 r
2.6.1.42 L-threonine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 2-oxo-3-hydroxybutyrate + L-leucine
-
 r
2.6.1.42 L-threonine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 768-28 2-oxo-3-hydroxybutyrate + L-leucine
-
 r
2.6.1.42 L-tryptophan + 2-oxoglutarate
-
 Escherichia coli 2-oxo-3-indolylpropanoate + L-glutamate
-
 r
2.6.1.42 L-tryptophan + 2-oxoglutarate
-
 Pseudomonas sp. 2-oxo-3-indolylpropanoate + L-glutamate
-
 r
2.6.1.42 L-tryptophan + 2-oxoglutarate
-
 Gluconobacter oxydans 2-oxo-3-indolylpropanoate + L-glutamate
-
 r
2.6.1.42 L-tryptophan + 2-oxoglutarate
-
 Brevibacillus brevis 2-oxo-3-indolylpropanoate + L-glutamate
-
 r
2.6.1.42 L-tryptophan + 2-oxoglutarate
-
 Methanococcus aeolicus 2-oxo-3-indolylpropanoate + L-glutamate
-
 r
2.6.1.42 L-tryptophan + 2-oxoglutarate
-
 Methanococcus aeolicus DSM 17508 2-oxo-3-indolylpropanoate + L-glutamate
-
 r
2.6.1.42 L-tryptophan + 2-oxoglutarate
-
 Methanococcus aeolicus ATCC BAA-1280 2-oxo-3-indolylpropanoate + L-glutamate
-
 r
2.6.1.42 L-tryptophan + 2-oxoglutarate
-
 Methanococcus aeolicus OCM 812 2-oxo-3-indolylpropanoate + L-glutamate
-
 r
2.6.1.42 L-tryptophan + 2-oxoglutarate
-
 Methanococcus aeolicus Nankai-3 2-oxo-3-indolylpropanoate + L-glutamate
-
 r
2.6.1.42 L-tryptophan + pyruvate
-
 Vulcanisaeta moutnovskia 2-oxo-3-indolylpropanoate + L-alanine
-
 r
2.6.1.42 L-tryptophan + pyruvate
-
 Thermococcus sp. CKU-1 2-oxo-3-indolylpropanoate + L-alanine
-
 r
2.6.1.42 L-tyrosine + 2-oxoglutarate
-
 Escherichia coli 4-hydroxyphenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-tyrosine + 2-oxoglutarate
-
 Brevibacillus brevis 4-hydroxyphenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-tyrosine + 2-oxoglutarate
-
 Methanococcus aeolicus 4-hydroxyphenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-tyrosine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 4-hydroxyphenylpyruvate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Escherichia coli 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Pseudomonas aeruginosa 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Pseudomonas sp. 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Gluconobacter oxydans 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Lactococcus lactis 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Lacticaseibacillus paracasei 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Brevibacillus brevis 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Helicobacter pylori 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Mycobacterium tuberculosis 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Methanococcus aeolicus 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Thermococcus sp. CKU-1 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Mycobacterium tuberculosis H37Rv 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Gluconobacter oxydans 621H 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Pseudomonas aeruginosa ATCC 15692 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Mycobacterium tuberculosis ATCC 25618 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Helicobacter pylori ATCC 700392 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 768-20 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Pseudomonas aeruginosa DSM 22644 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Methanococcus aeolicus DSM 17508 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Helicobacter pylori 26695 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Pseudomonas aeruginosa CIP 104116 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Pseudomonas aeruginosa JCM 14847 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Pseudomonas aeruginosa LMG 12228 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Pseudomonas aeruginosa 1C 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Pseudomonas aeruginosa PRS 101 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Methanococcus aeolicus ATCC BAA-1280 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Methanococcus aeolicus OCM 812 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Methanococcus aeolicus Nankai-3 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 3-methyl-2-oxobutanoate + L-leucine
-
 r
2.6.1.42 L-valine + 4-methyl-2-oxovalerate
-
 Vulcanisaeta moutnovskia 768-28 3-methyl-2-oxobutanoate + L-leucine
-
 r
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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. ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 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 ?
-
 ?
2.6.1.42 norleucine + 2-oxoglutarate
-
 Gluconobacter oxydans 2-oxohexanoate + L-glutamate
-
 r
2.6.1.42 norleucine + 2-oxoglutarate
-
 Brevibacillus brevis 2-oxohexanoate + L-glutamate
-
 r
2.6.1.42 norleucine + 2-oxoglutarate
-
 Thermoproteus uzoniensis 2-oxohexanoate + L-glutamate
-
 r
2.6.1.42 norvaline + 2-oxoglutarate
-
 Pseudomonas aeruginosa 2-oxovalerate + L-glutamate
-
 r
2.6.1.42 norvaline + 2-oxoglutarate
-
 Gluconobacter oxydans 2-oxovalerate + L-glutamate
-
 r
2.6.1.42 norvaline + 2-oxoglutarate
-
 Brevibacillus brevis 2-oxovalerate + L-glutamate
-
 r
2.6.1.42 norvaline + 2-oxoglutarate
-
 Thermoproteus uzoniensis 2-oxovalerate + L-glutamate
-
 r
2.6.1.42 norvaline + 2-oxoglutarate
-
 Thermoproteus uzoniensis 768-20 2-oxovalerate + L-glutamate
-
 r
2.6.1.42 pyruvate + L-alanine
-
 Thermoproteus uzoniensis L-alanine + pyruvate
-
 r
2.6.1.42 pyruvate + L-alanine
-
 Vulcanisaeta moutnovskia L-alanine + pyruvate
-
 r
2.6.1.42 pyruvate + L-glutamate
-
 Pseudomonas sp. L-alanine + 2-oxoglutarate
-
 r
2.6.1.42 pyruvate + L-glutamate low activity Lactococcus lactis L-alanine + 2-oxoglutarate
-
 r
2.6.1.42 pyruvate + L-glutamate low activity Lacticaseibacillus paracasei L-alanine + 2-oxoglutarate
-
 r
2.6.1.42 trimethylpyruvate + L-glutamate
-
 Escherichia coli L-tert-Leu + 2-oxoglutarate
-
 r

Subunits

EC Number Subunits Comment Organism
2.6.1.42 ? x * 37800, SDS-PAGE Lacticaseibacillus paracasei
2.6.1.42 homodimer 2 * 39000, SDS-PAGE Gluconobacter oxydans
2.6.1.42 homodimer 2 * 37400, SDS-PAGE Lactococcus lactis
2.6.1.42 homodimer 2 * 40100, SDS-PAGE Brevibacillus brevis
2.6.1.42 homodimer 2 * 37500, SDS-PAGE Helicobacter pylori
2.6.1.42 homodimer 2 * 34000, SDS-PAGE Mycobacterium tuberculosis
2.6.1.42 homodimer 2 * 32800, SDS-PAGE Thermoproteus uzoniensis
2.6.1.42 homodimer 2 * 47500, SDS-PAGE Thermococcus sp. CKU-1
2.6.1.42 homohexamer 6 * 34000, SDS-PAGE Escherichia coli
2.6.1.42 homohexamer 6 * 31800, SDS-PAGE Methanococcus aeolicus
2.6.1.42 homotetramer 4 * 34000, SDS-PAGE Pseudomonas aeruginosa
2.6.1.42 homotetramer 4 * 35300, SDS-PAGE Vulcanisaeta moutnovskia

Synonyms

EC Number Synonyms Comment Organism
2.6.1.42 BcaT
-
 Escherichia coli
2.6.1.42 BcaT
-
 Pseudomonas aeruginosa
2.6.1.42 BcaT
-
 Pseudomonas sp.
2.6.1.42 BcaT
-
 Gluconobacter oxydans
2.6.1.42 BcaT
-
 Lactococcus lactis
2.6.1.42 BcaT
-
 Lacticaseibacillus paracasei
2.6.1.42 BcaT
-
 Brevibacillus brevis
2.6.1.42 BcaT
-
 Helicobacter pylori
2.6.1.42 BcaT
-
 Mycobacterium tuberculosis
2.6.1.42 BcaT
-
 Methanococcus aeolicus
2.6.1.42 BcaT
-
 Thermoproteus uzoniensis
2.6.1.42 BcaT
-
 Vulcanisaeta moutnovskia
2.6.1.42 BcaT
-
 Thermococcus sp. CKU-1
2.6.1.42 branched-chain amino acid aminotransferase
-
 Escherichia coli
2.6.1.42 branched-chain amino acid aminotransferase
-
 Pseudomonas aeruginosa
2.6.1.42 branched-chain amino acid aminotransferase
-
 Pseudomonas sp.
2.6.1.42 branched-chain amino acid aminotransferase
-
 Gluconobacter oxydans
2.6.1.42 branched-chain amino acid aminotransferase
-
 Lactococcus lactis
2.6.1.42 branched-chain amino acid aminotransferase
-
 Lacticaseibacillus paracasei
2.6.1.42 branched-chain amino acid aminotransferase
-
 Brevibacillus brevis
2.6.1.42 branched-chain amino acid aminotransferase
-
 Helicobacter pylori
2.6.1.42 branched-chain amino acid aminotransferase
-
 Mycobacterium tuberculosis
2.6.1.42 branched-chain amino acid aminotransferase
-
 Methanococcus aeolicus
2.6.1.42 branched-chain amino acid aminotransferase
-
 Thermoproteus uzoniensis
2.6.1.42 branched-chain amino acid aminotransferase
-
 Vulcanisaeta moutnovskia
2.6.1.42 branched-chain amino acid aminotransferase
-
 Thermococcus sp. CKU-1
2.6.1.42 eBCAT
-
 Escherichia coli
2.6.1.42 IlvE
-
 Escherichia coli
2.6.1.42 IlvE
-
 Pseudomonas aeruginosa
2.6.1.42 IlvE
-
 Gluconobacter oxydans
2.6.1.42 IlvE
-
 Lactococcus lactis
2.6.1.42 IlvE
-
 Lacticaseibacillus paracasei
2.6.1.42 IlvE
-
 Helicobacter pylori
2.6.1.42 IlvE
-
 Mycobacterium tuberculosis
2.6.1.42 IlvE
-
 Methanococcus aeolicus
2.6.1.42 IlvE
-
 Thermoproteus uzoniensis
2.6.1.42 IlvE
-
 Vulcanisaeta moutnovskia
2.6.1.42 IlvE
-
 Thermococcus sp. CKU-1

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.42 25
-
 assay at Escherichia coli
2.6.1.42 30
-
 assay at Pseudomonas sp.
2.6.1.42 37
-
 assay at Brevibacillus brevis
2.6.1.42 37
-
 assay at Gluconobacter oxydans
2.6.1.42 37
-
 assay at Helicobacter pylori
2.6.1.42 37
-
 assay at Lacticaseibacillus paracasei
2.6.1.42 37
-
 assay at Lactococcus lactis
2.6.1.42 37
-
 assay at Methanococcus aeolicus
2.6.1.42 37
-
 assay at Mycobacterium tuberculosis
2.6.1.42 37
-
 assay at Pseudomonas aeruginosa
2.6.1.42 65
-
 assay at Thermoproteus uzoniensis
2.6.1.42 65
-
 assay at Vulcanisaeta moutnovskia
2.6.1.42 90
-
 assay at Thermococcus sp. CKU-1

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.42 0.07
-
 3-methyl-2-oxopentanoate pH 8.0, 25°C Escherichia coli
2.6.1.42 0.08
-
 4-methyl-2-oxopentanoate pH 8.0, 25°C Escherichia coli
2.6.1.42 0.08
-
 4,4-dimethyl-2-oxovalerate pH 8.0, 25°C Escherichia coli
2.6.1.42 0.15
-
 trimethylpyruvate pH 8.0, 25°C Escherichia coli
2.6.1.42 0.2
-
 3-methyl-2-oxobutanoate pH 8.0, 25°C Escherichia coli
2.6.1.42 0.22
-
 2-Oxohexanoate pH 8.0, 25°C Escherichia coli
2.6.1.42 0.6
-
 2-oxovalerate pH 8.0, 25°C Escherichia coli
2.6.1.42 3.37
-
 2-oxobutyrate pH 8.0, 25°C Escherichia coli
2.6.1.42 48
-
 L-leucine pH 8.0, 25°C Escherichia coli
2.6.1.42 48
-
 L-isoleucine pH 8.0, 25°C Escherichia coli
2.6.1.42 56
-
 pyruvate pH 8.0, 25°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.42 7.3
-
 assay at Thermococcus sp. CKU-1
2.6.1.42 7.4
-
 assay at Lacticaseibacillus paracasei
2.6.1.42 7.4
-
 assay at Mycobacterium tuberculosis
2.6.1.42 7.5
-
 assay at Lactococcus lactis
2.6.1.42 7.5
-
 assay at Methanococcus aeolicus
2.6.1.42 8
-
 assay at Escherichia coli
2.6.1.42 8
-
 assay at Pseudomonas aeruginosa
2.6.1.42 8
-
 assay at Pseudomonas sp.
2.6.1.42 8
-
 assay at Brevibacillus brevis
2.6.1.42 8
-
 assay at Helicobacter pylori
2.6.1.42 8
-
 assay at Thermoproteus uzoniensis
2.6.1.42 8
-
 assay at Vulcanisaeta moutnovskia
2.6.1.42 9
-
 assay at Gluconobacter oxydans

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Escherichia coli
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Pseudomonas aeruginosa
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Pseudomonas sp.
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Gluconobacter oxydans
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Lactococcus lactis
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Lacticaseibacillus paracasei
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Brevibacillus brevis
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Helicobacter pylori
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Mycobacterium tuberculosis
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Methanococcus aeolicus
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Thermoproteus uzoniensis
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Vulcanisaeta moutnovskia
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Thermococcus sp. CKU-1

General Information

EC Number General Information Comment Organism
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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.
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Escherichia coli
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Pseudomonas aeruginosa
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Pseudomonas sp.
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Gluconobacter oxydans
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Lactococcus lactis
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Lacticaseibacillus paracasei
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Brevibacillus brevis
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Helicobacter pylori
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Mycobacterium tuberculosis
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Methanococcus aeolicus
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Thermoproteus uzoniensis
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Vulcanisaeta moutnovskia
2.6.1.42 metabolism BCAT are the key enzymes of BCAA metabolism in all organisms Thermococcus sp. CKU-1
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Escherichia coli
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Pseudomonas aeruginosa
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Pseudomonas sp.
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Gluconobacter oxydans
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Lactococcus lactis
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Lacticaseibacillus paracasei
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Brevibacillus brevis
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Helicobacter pylori
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Mycobacterium tuberculosis
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Methanococcus aeolicus
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Thermoproteus uzoniensis
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Vulcanisaeta moutnovskia
2.6.1.42 additional information structure-function analysis and substrate specificity, comparisons, overview Thermococcus sp. CKU-1
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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.
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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
2.6.1.42 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