Chemical modification of histidyl and lysyl residues in yeast enolse

Alfred L. George*, C. L. Borders

*Corresponding author for this work

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Modification of yeast enolase (2-phospho-d-glycerate, hydro-lyase, EC 4.2.1.11) by diethyl pyrocarbonate at either pH 6.1 or 6.6 caused a biphasic inactivation of the enzyme. In the presence of excess Mg2+, either an equilibrium mixture of substrates or 3-phosphoglycerate, a competitive inhibitor, prevented the second slower phase of inactivation, but had no effect on the first rapid phase. Complete inactivation by diethyl pyrocarbonate correlates with the modification of six histidyl residues/subunit, while 3-phosphoglycerate protects two histidyl residues/subunit from modification. Modification of enolase by two lysine-specific reagents, 2,4,6-trinitrobenzenesulfonate and pyridoxal 5′-phosphate, at pH 8.3 caused a slow loss of enzyme activity. However, substrates did not significantly protect against inactivation by either reagent, and inactivation with 2,4,6-trinitrobenzenesulfonate correlates with the modification of 18 lysyl residues/enzyme subunit.

Original languageEnglish (US)
Pages (from-to)63-69
Number of pages7
JournalBBA - Enzymology
Volume569
Issue number1
DOIs
StatePublished - Jul 11 1979

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Diethyl Pyrocarbonate
Phosphopyruvate Hydratase
Yeasts
Enzymes
Hydro-Lyases
Pyridoxal Phosphate
Lysine
3-phosphoglycerate

Keywords

  • (Yeast)
  • Chemical modification
  • Diethyl pyrocarbonate
  • Enolase
  • Histidine
  • Lysine

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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title = "Chemical modification of histidyl and lysyl residues in yeast enolse",
abstract = "Modification of yeast enolase (2-phospho-d-glycerate, hydro-lyase, EC 4.2.1.11) by diethyl pyrocarbonate at either pH 6.1 or 6.6 caused a biphasic inactivation of the enzyme. In the presence of excess Mg2+, either an equilibrium mixture of substrates or 3-phosphoglycerate, a competitive inhibitor, prevented the second slower phase of inactivation, but had no effect on the first rapid phase. Complete inactivation by diethyl pyrocarbonate correlates with the modification of six histidyl residues/subunit, while 3-phosphoglycerate protects two histidyl residues/subunit from modification. Modification of enolase by two lysine-specific reagents, 2,4,6-trinitrobenzenesulfonate and pyridoxal 5′-phosphate, at pH 8.3 caused a slow loss of enzyme activity. However, substrates did not significantly protect against inactivation by either reagent, and inactivation with 2,4,6-trinitrobenzenesulfonate correlates with the modification of 18 lysyl residues/enzyme subunit.",
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author = "George, {Alfred L.} and Borders, {C. L.}",
year = "1979",
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language = "English (US)",
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Chemical modification of histidyl and lysyl residues in yeast enolse. / George, Alfred L.; Borders, C. L.

In: BBA - Enzymology, Vol. 569, No. 1, 11.07.1979, p. 63-69.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Chemical modification of histidyl and lysyl residues in yeast enolse

AU - George, Alfred L.

AU - Borders, C. L.

PY - 1979/7/11

Y1 - 1979/7/11

N2 - Modification of yeast enolase (2-phospho-d-glycerate, hydro-lyase, EC 4.2.1.11) by diethyl pyrocarbonate at either pH 6.1 or 6.6 caused a biphasic inactivation of the enzyme. In the presence of excess Mg2+, either an equilibrium mixture of substrates or 3-phosphoglycerate, a competitive inhibitor, prevented the second slower phase of inactivation, but had no effect on the first rapid phase. Complete inactivation by diethyl pyrocarbonate correlates with the modification of six histidyl residues/subunit, while 3-phosphoglycerate protects two histidyl residues/subunit from modification. Modification of enolase by two lysine-specific reagents, 2,4,6-trinitrobenzenesulfonate and pyridoxal 5′-phosphate, at pH 8.3 caused a slow loss of enzyme activity. However, substrates did not significantly protect against inactivation by either reagent, and inactivation with 2,4,6-trinitrobenzenesulfonate correlates with the modification of 18 lysyl residues/enzyme subunit.

AB - Modification of yeast enolase (2-phospho-d-glycerate, hydro-lyase, EC 4.2.1.11) by diethyl pyrocarbonate at either pH 6.1 or 6.6 caused a biphasic inactivation of the enzyme. In the presence of excess Mg2+, either an equilibrium mixture of substrates or 3-phosphoglycerate, a competitive inhibitor, prevented the second slower phase of inactivation, but had no effect on the first rapid phase. Complete inactivation by diethyl pyrocarbonate correlates with the modification of six histidyl residues/subunit, while 3-phosphoglycerate protects two histidyl residues/subunit from modification. Modification of enolase by two lysine-specific reagents, 2,4,6-trinitrobenzenesulfonate and pyridoxal 5′-phosphate, at pH 8.3 caused a slow loss of enzyme activity. However, substrates did not significantly protect against inactivation by either reagent, and inactivation with 2,4,6-trinitrobenzenesulfonate correlates with the modification of 18 lysyl residues/enzyme subunit.

KW - (Yeast)

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KW - Diethyl pyrocarbonate

KW - Enolase

KW - Histidine

KW - Lysine

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