Literature summary for 2.6.1.1 extracted from

Birolo, L.; Malashkevich, V.N.; Capitani, G.; De Luca, F.; Moretta, A.; Jansonius, J.N.; Marino, G.
Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase (1999), Biochemistry, 38, 905-913.

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapour diffusion, crystals of mutants P195A and P138A/P195A in complex with maleate, protein solution: 20 mg/ml, 10 mM potassium phosphate, 0.01 mM pyridoxal 5'-phosphate, 2 mM EDTA, 0.5 mM DTT, reservoir solution: 1.9-2.1 M ammonium sulfate, 0.2 M 2-methylmorpholine, 2% polyethylene glycol 400, mutant P138A/P195A is also crystallized in complex with maleate, 20 mM, X-ray diffraction structure analysis	Escherichia coli

Crystallization (Comment)

Organism

hanging drop vapour diffusion, crystals of mutants P195A and P138A/P195A in complex with maleate, protein solution: 20 mg/ml, 10 mM potassium phosphate, 0.01 mM pyridoxal 5'-phosphate, 2 mM EDTA, 0.5 mM DTT, reservoir solution: 1.9-2.1 M ammonium sulfate, 0.2 M 2-methylmorpholine, 2% polyethylene glycol 400, mutant P138A/P195A is also crystallized in complex with maleate, 20 mM, X-ray diffraction structure analysis

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
P138A	oligonucleotide-directed mutagenesis, no significant effect, unaltered compared to the wild-type	Escherichia coli
P138A/P195A	oligonucleotide-directed mutagenesis	Escherichia coli
P195A	oligonucleotide-directed mutagenesis, no significant effect, unaltered compared to the wild-type	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-aspartate + 2-oxoglutarate	Escherichia coli	-	oxaloacetate + L-glutamate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P00509	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
wild-type and mutants, unfolding by guanidinium hydrochloride and renaturing kinetics, fluorescent spectrometric analysis	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate + 2-oxoglutarate	-	Escherichia coli	oxaloacetate + L-glutamate	-	?
L-aspartate + 2-oxoglutarate	-	Escherichia coli	oxaloacetate + L-glutamate	-	r

Synonyms

Synonyms	Comment	Organism
AspAT	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Escherichia coli