Essential arginyl residues in yeast enolase

C. L. Borders*, Mary L. Woodall, Alfred L. George

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Yeast enolase is rapidly inactivated by butanedione in borate buffer, complete inactivation correlating with the modification of 1. 8 arginyl residues per subunit. Protection against inactivation is provided by either an equilibrium mixture of substrates or inorganic phosphate, a competitive inhibitor of the enzyme. Complete protection by substrates correlates with the shielding of 1. 3 arginyl residues per subunit, while phosphate protects 1. 0 arginyl residue per subunit from modification.

Original languageEnglish (US)
Pages (from-to)901-906
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume82
Issue number3
DOIs
StatePublished - Jun 14 1978

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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