Identification of an essential residue of pig heart aconitase

Treatment of aconitase with phenacyl bromide prior to activation with Fe(II) and reductant results in complete, irreversible enzyme inactivation. Inactivation is due to the alkylation of a cysteine residue at the active site of the enzyme, the inactivation being inhibited by the competitive inhibito...

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Veröffentlicht in:Biochemical and biophysical research communications 1977-01, Vol.74 (2), p.384-389
Hauptverfasser: Johnson, Paul G., Waheed, Abdul, Jones, Laudie, Glaid, A.J., Gawron, Oscar
Format: Artikel
Sprache:eng
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Zusammenfassung:Treatment of aconitase with phenacyl bromide prior to activation with Fe(II) and reductant results in complete, irreversible enzyme inactivation. Inactivation is due to the alkylation of a cysteine residue at the active site of the enzyme, the inactivation being inhibited by the competitive inhibitor, tricarballylate. Active enzyme is similarly inactivated, citrate affording greater protection than tricarballylate.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(77)90315-1