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Literature summary extracted from

  • Bezsudnova, E.Y.; Stekhanova, T.N.; Suplatov, D.A.; Mardanov, A.V.; Ravin, N.V.; Popov, V.O.
    Experimental and computational studies on the unusual substrate specificity of branched-chain amino acid aminotransferase from Thermoproteus uzoniensis (2016), Arch. Biochem. Biophys., 607, 27-36 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.42 3-methyl-2-oxovalerate enzyme TUZN1299 is inhibited by keto acceptors in substrate inhibition, the maximum activity toward 4-methyl-2-oxovalerate and 3-methyl-2-oxovalerate in the reaction with L-alanine is achieved at a concentration of keto acids 1 mM, at 20 mM the specific activity of the enzyme decreases by 60% and 80%, respectively Thermoproteus uzoniensis
2.6.1.42 4-methyl-2-oxovalerate enzyme TUZN1299 is inhibited by keto acceptors in substrate inhibition, the maximum activity toward 4-methyl-2-oxovalerate and 3-methyl-2-oxovalerate in the reaction with L-alanine is achieved at a concentration of keto acids 1 mM, at 20 mM the specific activity of the enzyme decreases by 60% and 80%, respectively Thermoproteus uzoniensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.42 additional information
-
 additional information stopped-flow kinetics analysis of half-transamination reactions, steady-state kinetics Thermoproteus uzoniensis
2.6.1.42 0.15
-
 4-methyl-2-oxopentanoate pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 0.21
-
 L-leucine pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 16
-
 pyruvate pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 62
-
 L-alanine pH 8.0, 65°C Thermoproteus uzoniensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.42 L-isoleucine + 2-oxobutyrate Thermoproteus uzoniensis
-
 3-methyl-2-oxopentanoate + 2-aminobutyrate
-
 r
2.6.1.42 L-isoleucine + 2-oxobutyrate Thermoproteus uzoniensis 768-20
-
 3-methyl-2-oxopentanoate + 2-aminobutyrate
-
 r
2.6.1.42 L-leucine + 2-oxobutyrate Thermoproteus uzoniensis
-
 4-methyl-2-oxopentanoate + 2-aminobutyrate
-
 r
2.6.1.42 L-valine + 2-oxobutyrate Thermoproteus uzoniensis
-
 3-methyl-2-oxobutanoate + 2-aminobutyrate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.42 Thermoproteus uzoniensis F2L0W0
-
-
2.6.1.42 Thermoproteus uzoniensis 768-20 F2L0W0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.42 4-methyl-2-oxopentanoate + L-alanine
-
 Thermoproteus uzoniensis L-leucine + pyruvate
-
 r
2.6.1.42 4-methyl-2-oxopentanoate + L-alanine
-
 Thermoproteus uzoniensis 768-20 L-leucine + pyruvate
-
 r
2.6.1.42 L-glutamine + 2-oxobutyrate
-
 Thermoproteus uzoniensis 2,5-dioxo-5-aminopentanoate + 2-aminobutyrate
-
 r
2.6.1.42 L-homoserine + 2-oxobutyrate
-
 Thermoproteus uzoniensis ? + 2-aminobutyrate
-
 r
2.6.1.42 L-isoleucine + 2-oxobutyrate
-
 Thermoproteus uzoniensis 3-methyl-2-oxopentanoate + 2-aminobutyrate
-
 r
2.6.1.42 L-isoleucine + 2-oxobutyrate
-
 Thermoproteus uzoniensis 768-20 3-methyl-2-oxopentanoate + 2-aminobutyrate
-
 r
2.6.1.42 L-leucine + 2-oxobutyrate
-
 Thermoproteus uzoniensis 4-methyl-2-oxopentanoate + 2-aminobutyrate
-
 r
2.6.1.42 L-leucine + pyruvate
-
 Thermoproteus uzoniensis 4-methyl-2-oxopentanoate + L-alanine
-
 r
2.6.1.42 L-leucine + pyruvate
-
 Thermoproteus uzoniensis 768-20 4-methyl-2-oxopentanoate + L-alanine
-
 r
2.6.1.42 L-methionine + 2-oxobutyrate
-
 Thermoproteus uzoniensis 4-methylsulfanyl-2-oxobutanoate + 2-aminobutyrate
-
 r
2.6.1.42 L-methionine + 2-oxobutyrate
-
 Thermoproteus uzoniensis 768-20 4-methylsulfanyl-2-oxobutanoate + 2-aminobutyrate
-
 r
2.6.1.42 L-threonine + 2-oxobutyrate
-
 Thermoproteus uzoniensis 2-oxo-3-hydroxybutyrate + 2-aminobutyrate
-
 r
2.6.1.42 L-valine + 2-oxobutyrate
-
 Thermoproteus uzoniensis 3-methyl-2-oxobutanoate + 2-aminobutyrate
-
 r
2.6.1.42 additional information enzyme TUZN1299 is highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, L-methionine, L-threonine, L-homoserine, L-glutamine, as well as toward 2-oxobutyrate and keto analogues of BCAAs, whereas L-glutamate and 2-oxoglutarate are not converted in the overall reaction. The enzyme shows the highest specificity to BCAAs and their keto analogues. Glu188 forms a novel binding site for positively charged and polar side-chains of amino acids. Lack of accommodation for 2-oxoglutarate and L-glutamate is due to the unique orientation and chemical properties of residues 102-106 in the loop forming the A-pocket, molecular modelling and molecular mechanism, overview. The productive binding of 2-oxooglutarate and L-glutamate (both featuring negatively charged side-chains) in the active site of PMP-enzyme and PLP-enzyme models, respectively, is not observed Thermoproteus uzoniensis ?
-
-
2.6.1.42 additional information enzyme TUZN1299 is highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, L-methionine, L-threonine, L-homoserine, L-glutamine, as well as toward 2-oxobutyrate and keto analogues of BCAAs, whereas L-glutamate and 2-oxoglutarate are not converted in the overall reaction. The enzyme shows the highest specificity to BCAAs and their keto analogues. Glu188 forms a novel binding site for positively charged and polar side-chains of amino acids. Lack of accommodation for 2-oxoglutarate and L-glutamate is due to the unique orientation and chemical properties of residues 102-106 in the loop forming the A-pocket, molecular modelling and molecular mechanism, overview. The productive binding of 2-oxooglutarate and L-glutamate (both featuring negatively charged side-chains) in the active site of PMP-enzyme and PLP-enzyme models, respectively, is not observed Thermoproteus uzoniensis 768-20 ?
-
-

Synonyms

EC Number Synonyms Comment Organism
2.6.1.42 BcaT
-
 Thermoproteus uzoniensis
2.6.1.42 branched-chain amino acid aminotransferase
-
 Thermoproteus uzoniensis
2.6.1.42 TUZN1299
-
 Thermoproteus uzoniensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.42 65
-
 assay at Thermoproteus uzoniensis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.42 1.31
-
 L-leucine pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 1.78
-
 pyruvate pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 2.7
-
 L-alanine pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 3
-
 4-methyl-2-oxopentanoate pH 8.0, 65°C Thermoproteus uzoniensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.42 8
-
 assay at Thermoproteus uzoniensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.6.1.42 6 10 the enzyme activity increases from pH 6.0 to pH 10.0 at 65°C Thermoproteus uzoniensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.42 pyridoxal 5'-phosphate PLP, dependent on Thermoproteus uzoniensis

General Information

EC Number General Information Comment Organism
2.6.1.42 evolution the enzyme belongs to the PLP-dependent fold-type IV branched-chain amino acid aminotransferases (BCATs) from archaea, docking study and identification of subfamily-specific positions, overview Thermoproteus uzoniensis
2.6.1.42 additional information molecular docking of 2-oxoglutarate, L-ornithine and L-glutamate into the molecular model of TUZN1299 Thermoproteus uzoniensis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.6.1.42 0.044
-
 L-alanine pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 0.11
-
 pyruvate pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 6.24
-
 L-leucine pH 8.0, 65°C Thermoproteus uzoniensis
2.6.1.42 20
-
 4-methyl-2-oxopentanoate pH 8.0, 65°C Thermoproteus uzoniensis