Essential arginyl residues in yeast enolase

C. L. Borders; Mary L. Woodall; Alfred L. George

doi:10.1016/0006-291X(78)90868-9

Essential arginyl residues in yeast enolase

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

^*Corresponding author for this work

Pharmacology

Research output: Contribution to journal › Article › peer-review

20 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 language	English (US)
Pages (from-to)	901-906
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	82
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(78)90868-9
State	Published - Jun 14 1978

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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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.",

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AU - Woodall, Mary L.

AU - George, Alfred L.

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AB - 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.

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Essential arginyl residues in yeast enolase

Abstract

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