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Literature summary for 2.6.1.79 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
Search for more literature for 2.6.1.79

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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
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

Protein Variants Comment Organism
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten steady-state kinetics analysis Sinorhizobium meliloti

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arogenate + 2-oxoglutarate Arabidopsis thaliana
-
 L-glutamate + prephenate
-
 r
L-arogenate + 2-oxoglutarate Sinorhizobium meliloti
-
 L-glutamate + prephenate
-
 r

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9SIE1
-
-
Sinorhizobium meliloti Q02635
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arogenate + 2-oxoglutarate
-
 Arabidopsis thaliana L-glutamate + prephenate
-
 r
L-arogenate + 2-oxoglutarate
-
 Sinorhizobium meliloti L-glutamate + prephenate
-
 r
L-glutamate + prephenate
-
 Sinorhizobium meliloti L-arogenate + 2-oxoglutarate
-
 r

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Sinorhizobium meliloti

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Sinorhizobium meliloti

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Arabidopsis thaliana
pyridoxal 5'-phosphate
-
 Sinorhizobium meliloti

General Information

General Information Comment Organism
malfunction one PAT incompetent 1beta AAT mutant K12G from Rhizobium meliloti is detected (UniProt ID P58350) Sinorhizobium meliloti
metabolism the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview Arabidopsis thaliana
metabolism the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview Sinorhizobium meliloti
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
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