Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.6.1.1 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
Search for more literature for 2.6.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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
DELTA1-7 truncation of the first seven amino acids only minorly reduces enzymatic activity Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
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

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

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum O96142
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer
-
 Plasmodium falciparum

Synonyms

Synonyms Comment Organism
AspAT
-
 Plasmodium falciparum

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Plasmodium falciparum

IC50 Value

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