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Literature summary extracted from

  • Alvarez, C.; Lozano-Juste, J.; Romero, L.C.; Garcia, I.; Gotor, C.; Leon, J.
    Inhibition of Arabidopsis O-acetylserine(thiol)lyase A1 by tyrosine nitration (2011), J. Biol. Chem., 286, 578-586.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.47 Y302A loss of enzymic activity Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.47 peroxynitrite nitrating conditions after exposure to peroxynitrite strongly inhibit enzyme activity. Among the isoforms, cytosolic OASA1 is markedly sensitive to nitration. Nitration assays on purified recombinant OASA1 protein lead to 90% reduction of the activity due to inhibition of the enzyme. Inhibition of OASA1 activity upon nitration correlates with the identification of a modified OASA1 protein containing a 3-nitroTyr302 residue. Inhibition caused by Tyr302 nitration on OASA1 activity seems to be due to a drastically reduced O-acetylserine substrate binding to the nitrated protein, and also to reduced stabilization of the pyridoxal-5-phosphate cofactor through hydrogen bonds Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.5.1.47 cytosol
-
 Arabidopsis thaliana 5829
-

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Arabidopsis thaliana
-
-
-

Synonyms

EC Number Synonyms Comment Organism
2.5.1.47 OASA1
-
 Arabidopsis thaliana