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 (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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten steady-state kinetics analysis | Sinorhizobium meliloti |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | Q9SIE1 | - |
- |
Sinorhizobium meliloti | Q02635 | - |
- |
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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Sinorhizobium meliloti |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Sinorhizobium meliloti |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Arabidopsis thaliana | |
pyridoxal 5'-phosphate | - |
Sinorhizobium meliloti |
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 |