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Literature summary extracted from

  • Wrenger, C.; Mueller, I.B.; Schifferdecker, A.J.; Jain, R.; Jordanova, R.; Groves, M.R.
    Specific inhibition of the aspartate aminotransferase of Plasmodium falciparum (2011), J. Mol. Biol., 405, 956-971.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.1 the X-ray structure of the PfAspAT homodimer at a resolution of 2.8 A is reported. While the overall fold is similar to the currently available structures of other AspATs, the structure presented shows a significant divergence in the conformation of the N-terminal residues Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.1 DELTA1-13 truncation of these noncatalytic residues reduces enzyme activity and a peptide containing these amino acids inhibits PfAspAT in vitro and in the lysate of cultured parasites Plasmodium falciparum
2.6.1.1 DELTA1-7 truncation of the first seven amino acids only minorly reduces enzymatic activity Plasmodium falciparum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.1 hydroxylamine inhibition of PfAspAT abolishes all glutamate oxaloacetate transamination activity in the cytoplasm of cultured parasites, demonstrating that no other enzyme within the cytoplasm can complement PfAspAT activity Plasmodium falciparum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.6.1.1 cytoplasm
-
 Plasmodium falciparum 5737
-

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.1 Plasmodium falciparum O96142
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.1 0.14
-
 substrates: L-asparagine + 2-oxoglutarate, pH 8, 37°C Plasmodium falciparum
2.6.1.1 0.16
-
 substrates: L-tryptophan + 2-oxoglutarate, pH 8, 37°C Plasmodium falciparum
2.6.1.1 0.24
-
 substrates: L-tyrosine + 2-oxoglutarate, pH 8, 37°C Plasmodium falciparum
2.6.1.1 0.28
-
 substrates: L-phenylalanine + 2-oxoglutarate, pH 8, 37°C Plasmodium falciparum
2.6.1.1 2.67
-
 substrates: L-aspartate + 2-oxoglutarate, pH 8, 37°C Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.1 L-asparagine + 2-oxoglutarate specific activity: 0.14 micromol/min/mg Plasmodium falciparum 4-amino-2,4-dioxobutanoate + L-glutamate
-
 ?
2.6.1.1 L-aspartate + 2-oxoglutarate specific activity: 2.67 micromol/min/mg Plasmodium falciparum oxaloacetate + L-glutamate
-
 ?
2.6.1.1 L-phenylalanine + 2-oxoglutarate specific activity: 0.28 micromol/min/mg Plasmodium falciparum 2-oxo-3-phenylpropanoate + L-glutamate
-
 ?
2.6.1.1 L-tryptophan + 2-oxoglutarate specific activity: 0.16 micromol/min/mg Plasmodium falciparum 3-(1H-indol-3-yl)-2-oxopropanoate + L-glutamate
-
 ?
2.6.1.1 L-tyrosine + 2-oxoglutarate specific activity: 0.24 micromol/min/mg Plasmodium falciparum 3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.6.1.1 homodimer
-
 Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
2.6.1.1 AspAT
-
 Plasmodium falciparum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.1 37
-
 assay at Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.1 8
-
 assay at Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.1 pyridoxal 5'-phosphate
-
 Plasmodium falciparum

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.6.1.1 0.069
-
 pH 8, 37°C Plasmodium falciparum hydroxylamine