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Literature summary extracted from

  • Giustini, C.; Graindorge, M.; Cobessi, D.; Crouzy, S.; Robin, A.; Curien, G.; Matringe, M.
    Tyrosine metabolism identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase (2019), FEBS J., 286, 2118-2134 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.78 gene aat, recombinant expression in Escherichia coli strain BL21 (DE3) Rosetta2 Arabidopsis thaliana
2.6.1.78 gene aat, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Rosetta2 Thermus thermophilus
2.6.1.78 gene aat, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Rosetta2 Sinorhizobium meliloti
2.6.1.79 gene aat, recombinant expression in Escherichia coli strain BL21 (DE3) Rosetta2 Arabidopsis thaliana
2.6.1.79 gene aat, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Rosetta2 Sinorhizobium meliloti

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.78 purified recombinant enzyme, crystallization from 0.1 M Na-citrate, pH 4.0, 11% PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 1.7 A resolution Arabidopsis thaliana
2.6.1.78 purified recombinant enzyme, Rme-AAT/PAT crystals are obtained from 0.2 M ammonium formate, 19% PEG 3350, and Rme-AAT grow from 0.1 M Na acetate pH 4.5, 5% PEG 4000, protein concentration is 10 mg/ml, at 20°C, X-ray diffraction structure determination and analysis at 1.79-1.9 A resolution Sinorhizobium meliloti
2.6.1.79 purified recombinant enzyme, crystallization from 0.1 M Na-citrate, pH 4.0, 11% PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 1.7 A resolution Arabidopsis thaliana
2.6.1.79 purified recombinant enzyme, Rme-AAT/PAT crystals are obtained from 0.2 M ammonium formate, 19% PEG 3350, and Rme-AAT grow from 0.1 M Na acetate pH 4.5, 5% PEG 4000, protein concentration is 10 mg/ml, at 20°C, X-ray diffraction structure determination and analysis at 1.79-1.9 A resolution Sinorhizobium meliloti

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.78 K12G naturally occuring mutant, the incompetent PATs of Rhizobium meliloti (UniProt ID P58350) has a G instead of K12 and shows reduced PAT activity at prephenate concentrations up to 2.5 mM using a coupled assay method. The mutant shows reduced activity and altered kinetics compared to the wild-type Sinorhizobium meliloti
2.6.1.78 K12G site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type Thermus thermophilus
2.6.1.78 additional information site-directed mutagenesis, modeling, and molecular dynamics simulations reveal that K/R/Q12 residue (numbering according to Thermus thermophilus 1beta AAT) is a signature of the PAT function of 1bta AAT. It is present in the N-terminal flexible loop only in PAT competent 1beta-AAT and has a possible role in stabilizing prephenate by interacting with its 4-hydroxy group Sinorhizobium meliloti
2.6.1.79 K12G naturally occuring mutant, the incompetent PATs of Rhizobium meliloti (UniProt ID P58350) has a G instead of K12 and shows reduced PAT activity at prephenate concentrations up to 2.5 mM using a coupled assay method. The mutant shows reduced activity and altered kinetics compared to the wild-type Sinorhizobium meliloti
2.6.1.79 additional information site-directed mutagenesis, modeling, and molecular dynamics simulations reveal that K/R/Q12 residue (numbering according to Thermus thermophilus 1beta AAT) is a signature of the PAT function of 1beta AAT. It is present in the N-terminal flexible loop only in PAT competent 1beta-AAT and has a possible role in stabilizing prephenate by interacting with its 4-hydroxy group Sinorhizobium meliloti

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.78 additional information
-
 additional information Michaelis-Menten steady-state kinetics analysis Thermus thermophilus
2.6.1.78 additional information
-
 additional information Michaelis-Menten steady-state kinetics analysis Sinorhizobium meliloti
2.6.1.78 0.0121
-
 oxaloacetate pH 8.0, 30°C, wild-type enzyme Sinorhizobium meliloti
2.6.1.78 0.0196
-
 oxaloacetate pH 8.0, 30°C, mutant K12G Sinorhizobium meliloti
2.6.1.78 0.0253
-
 oxaloacetate pH 8.0, 30°C, wild-type enzyme Thermus thermophilus
2.6.1.78 0.0264
-
 oxaloacetate pH 8.0, 30°C, mutant K12G Thermus thermophilus
2.6.1.78 0.114
-
 prephenate pH 8.0, 30°C, wild-type enzyme Sinorhizobium meliloti
2.6.1.78 0.15
-
 prephenate pH 8.0, 30°C, wild-type enzyme Thermus thermophilus
2.6.1.78 0.632
-
 prephenate pH 8.0, 30°C, mutant K12G Sinorhizobium meliloti
2.6.1.78 2.332
-
 prephenate pH 8.0, 30°C, mutant K12G Thermus thermophilus
2.6.1.79 additional information
-
 additional information Michaelis-Menten steady-state kinetics analysis Sinorhizobium meliloti

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.78 L-arogenate + oxaloacetate Arabidopsis thaliana
-
 L-aspartate + prephenate
-
 r
2.6.1.78 L-arogenate + oxaloacetate Thermus thermophilus
-
 L-aspartate + prephenate
-
 r
2.6.1.78 L-arogenate + oxaloacetate Sinorhizobium meliloti
-
 L-aspartate + prephenate
-
 r
2.6.1.78 L-arogenate + oxaloacetate Thermus thermophilus DSM 579
-
 L-aspartate + prephenate
-
 r
2.6.1.78 L-arogenate + oxaloacetate Thermus thermophilus ATCC 27634
-
 L-aspartate + prephenate
-
 r
2.6.1.79 L-arogenate + 2-oxoglutarate Arabidopsis thaliana
-
 L-glutamate + prephenate
-
 r
2.6.1.79 L-arogenate + 2-oxoglutarate Sinorhizobium meliloti
-
 L-glutamate + prephenate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.78 Arabidopsis thaliana Q9SIE1
-
-
2.6.1.78 Sinorhizobium meliloti Q02635
-
-
2.6.1.78 Thermus thermophilus Q56232
-
-
2.6.1.78 Thermus thermophilus ATCC 27634 Q56232
-
-
2.6.1.78 Thermus thermophilus DSM 579 Q56232
-
-
2.6.1.79 Arabidopsis thaliana Q9SIE1
-
-
2.6.1.79 Sinorhizobium meliloti Q02635
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.78 L-arogenate + oxaloacetate
-
 Arabidopsis thaliana L-aspartate + prephenate
-
 r
2.6.1.78 L-arogenate + oxaloacetate
-
 Thermus thermophilus L-aspartate + prephenate
-
 r
2.6.1.78 L-arogenate + oxaloacetate
-
 Sinorhizobium meliloti L-aspartate + prephenate
-
 r
2.6.1.78 L-arogenate + oxaloacetate
-
 Thermus thermophilus DSM 579 L-aspartate + prephenate
-
 r
2.6.1.78 L-arogenate + oxaloacetate
-
 Thermus thermophilus ATCC 27634 L-aspartate + prephenate
-
 r
2.6.1.78 L-aspartate + prephenate
-
 Thermus thermophilus L-arogenate + oxaloacetate
-
 r
2.6.1.78 L-aspartate + prephenate
-
 Sinorhizobium meliloti L-arogenate + oxaloacetate
-
 r
2.6.1.78 L-aspartate + prephenate
-
 Thermus thermophilus DSM 579 L-arogenate + oxaloacetate
-
 r
2.6.1.78 L-aspartate + prephenate
-
 Thermus thermophilus ATCC 27634 L-arogenate + oxaloacetate
-
 r
2.6.1.79 L-arogenate + 2-oxoglutarate
-
 Arabidopsis thaliana L-glutamate + prephenate
-
 r
2.6.1.79 L-arogenate + 2-oxoglutarate
-
 Sinorhizobium meliloti L-glutamate + prephenate
-
 r
2.6.1.79 L-glutamate + prephenate
-
 Sinorhizobium meliloti L-arogenate + 2-oxoglutarate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.6.1.78 1beta AAT
-
 Arabidopsis thaliana
2.6.1.78 1beta AAT
-
 Thermus thermophilus
2.6.1.78 1beta AAT
-
 Sinorhizobium meliloti
2.6.1.78 1beta AAT prephenate aminotransferase
-
 Arabidopsis thaliana
2.6.1.78 1beta AAT prephenate aminotransferase
-
 Thermus thermophilus
2.6.1.78 1beta AAT prephenate aminotransferase
-
 Sinorhizobium meliloti
2.6.1.78 1beta aspartate aminotransferase
-
 Arabidopsis thaliana
2.6.1.78 1beta aspartate aminotransferase
-
 Thermus thermophilus
2.6.1.78 1beta aspartate aminotransferase
-
 Sinorhizobium meliloti
2.6.1.78 aatA
-
 Sinorhizobium meliloti
2.6.1.78 aspartate/prephenate aminotransferase UniProt Thermus thermophilus
2.6.1.78 aspartate/prephenate aminotransferase UniProt Sinorhizobium meliloti
2.6.1.78 aspC
-
 Thermus thermophilus
2.6.1.78 Ath-PAT
-
 Arabidopsis thaliana
2.6.1.78 bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase UniProt Arabidopsis thaliana
2.6.1.78 More cf. EC 2.6.1.1 Thermus thermophilus
2.6.1.78 More cf. EC 2.6.1.79 and EC 2.6.1.1 Arabidopsis thaliana
2.6.1.78 More cf. EC 2.6.1.79 and EC 2.6.1.1 Sinorhizobium meliloti
2.6.1.78 Pat
-
 Arabidopsis thaliana
2.6.1.78 Pat
-
 Thermus thermophilus
2.6.1.78 Pat
-
 Sinorhizobium meliloti
2.6.1.78 Rme-AAT
-
 Sinorhizobium meliloti
2.6.1.78 Tth-PAT
-
 Thermus thermophilus
2.6.1.79 1beta AAT
-
 Arabidopsis thaliana
2.6.1.79 1beta AAT
-
 Sinorhizobium meliloti
2.6.1.79 1beta AAT prephenate aminotransferase
-
 Arabidopsis thaliana
2.6.1.79 1beta AAT prephenate aminotransferase
-
 Sinorhizobium meliloti
2.6.1.79 1beta aspartate aminotransferase
-
 Sinorhizobium meliloti
2.6.1.79 aatA
-
 Sinorhizobium meliloti
2.6.1.79 aspartate/prephenate aminotransferase UniProt Sinorhizobium meliloti
2.6.1.79 Ath-PAT
-
 Arabidopsis thaliana
2.6.1.79 bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase UniProt Arabidopsis thaliana
2.6.1.79 More cf. EC 2.6.1.78 and EC 2.6.1.1 Arabidopsis thaliana
2.6.1.79 More cf. EC 2.6.1.78 and EC 2.6.1.1 Sinorhizobium meliloti
2.6.1.79 Pat
-
 Arabidopsis thaliana
2.6.1.79 Pat
-
 Sinorhizobium meliloti
2.6.1.79 Rme-AAT
-
 Sinorhizobium meliloti
2.6.1.79 Rme-AAT/PAT
-
 Sinorhizobium meliloti

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.78 30
-
 assay at Thermus thermophilus
2.6.1.78 30
-
 assay at Sinorhizobium meliloti
2.6.1.79 30
-
 assay at Sinorhizobium meliloti

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.78 4.8
-
 prephenate pH 8.0, 30°C, mutant K12G Thermus thermophilus
2.6.1.78 7.7
-
 prephenate pH 8.0, 30°C, wild-type enzyme Thermus thermophilus
2.6.1.78 12.3
-
 oxaloacetate pH 8.0, 30°C, mutant K12G Thermus thermophilus
2.6.1.78 32.2
-
 oxaloacetate pH 8.0, 30°C, wild-type enzyme Thermus thermophilus
2.6.1.78 38.6
-
 prephenate pH 8.0, 30°C, mutant K12G Sinorhizobium meliloti
2.6.1.78 42.3
-
 prephenate pH 8.0, 30°C, wild-type enzyme Sinorhizobium meliloti
2.6.1.78 140.2
-
 oxaloacetate pH 8.0, 30°C, mutant K12G Sinorhizobium meliloti
2.6.1.78 158.4
-
 oxaloacetate pH 8.0, 30°C, wild-type enzyme Sinorhizobium meliloti

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.78 8
-
 assay at Thermus thermophilus
2.6.1.78 8
-
 assay at Sinorhizobium meliloti
2.6.1.79 8
-
 assay at Sinorhizobium meliloti

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.78 pyridoxal 5'-phosphate
-
 Arabidopsis thaliana
2.6.1.78 pyridoxal 5'-phosphate
-
 Thermus thermophilus
2.6.1.78 pyridoxal 5'-phosphate
-
 Sinorhizobium meliloti
2.6.1.79 pyridoxal 5'-phosphate
-
 Arabidopsis thaliana
2.6.1.79 pyridoxal 5'-phosphate
-
 Sinorhizobium meliloti

General Information

EC Number General Information Comment Organism
2.6.1.78 malfunction one PAT incompetent 1beta AAT mutant K12G from Rhizobium meliloti is detected (UniProt ID P58350) Sinorhizobium meliloti
2.6.1.78 metabolism the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview Arabidopsis thaliana
2.6.1.78 metabolism the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview Thermus thermophilus
2.6.1.78 metabolism the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview Sinorhizobium meliloti
2.6.1.78 additional information modeling and molecular dynamic simulations. Identification of a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. A Lys/Arg/Gln residue in position 12 (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, can interact with the 4-hydroxyl group of the prephenate substrate, probably playing a central role in the acquisition of PAT activity by 1beta AAT. PAT enzyme structures comparisons, overview Arabidopsis thaliana
2.6.1.78 additional information modeling and molecular dynamic simulations. Identification of a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. A Lys/Arg/Gln residue in position 12 (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, can interact with the 4-hydroxyl group of the prephenate substrate, probably playing a central role in the acquisition of PAT activity by 1beta AAT. PAT enzyme structures comparisons, overview Thermus thermophilus
2.6.1.78 additional information modeling and molecular dynamic simulations. Identification of a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. A Lys/Arg/Gln residue in position 12 (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, can interact with the 4-hydroxyl group of the prephenate substrate, probably playing a central role in the acquisition of PAT activity by 1beta AAT. PAT enzyme structures comparisons, overview. Lys12 plays a specific role in prephenate binding by PAT competent 1beta AAT Sinorhizobium meliloti
2.6.1.79 malfunction one PAT incompetent 1beta AAT mutant K12G from Rhizobium meliloti is detected (UniProt ID P58350) Sinorhizobium meliloti
2.6.1.79 metabolism the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview Arabidopsis thaliana
2.6.1.79 metabolism the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview Sinorhizobium meliloti
2.6.1.79 additional information modeling and molecular dynamic simulations. Identification of a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. A Lys/Arg/Gln residue in position 12 (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, can interact with the 4-hydroxyl group of the prephenate substrate, probably playing a central role in the acquisition of PAT activity by 1beta AAT. PAT enzyme structures comparisons, overview Arabidopsis thaliana
2.6.1.79 additional information modeling and molecular dynamic simulations. Identification of a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. A Lys/Arg/Gln residue in position 12 (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, can interact with the 4-hydroxyl group of the prephenate substrate, probably playing a central role in the acquisition of PAT activity by 1beta AAT. PAT enzyme structures comparisons, overview. Lys12 plays a specific role in prephenate binding by PAT competent 1beta AAT Sinorhizobium meliloti

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.6.1.78 2.06
-
 prephenate pH 8.0, 30°C, mutant K12G Thermus thermophilus
2.6.1.78 51.3
-
 prephenate pH 8.0, 30°C, wild-type enzyme Thermus thermophilus
2.6.1.78 61.1
-
 prephenate pH 8.0, 30°C, mutant K12G Sinorhizobium meliloti
2.6.1.78 371.1
-
 prephenate pH 8.0, 30°C, wild-type enzyme Sinorhizobium meliloti
2.6.1.78 465.9
-
 oxaloacetate pH 8.0, 30°C, mutant K12G Thermus thermophilus
2.6.1.78 1272.7
-
 oxaloacetate pH 8.0, 30°C, wild-type enzyme Thermus thermophilus
2.6.1.78 7153.1
-
 oxaloacetate pH 8.0, 30°C, mutant K12G Sinorhizobium meliloti
2.6.1.78 13090.9
-
 oxaloacetate pH 8.0, 30°C, wild-type enzyme Sinorhizobium meliloti