Essential carboxyl residues in yeast enolase

Alfred L. George, C. L. Borders*

*Corresponding author for this work

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Yeast enolase (EC 4.2.1.11) is rapidly inactivated at pH 6.1 by three different water-soluble carbodiimides - 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide hydrochloride, 1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluenesulfonate, and 1-ethyl-3-(4-azonia-4,4-dimethylpentyl)-carbodiimide iodide. Inactivation is most likely due to the modification of essential carboxyl residues at the enzyme active site.

Original languageEnglish (US)
Pages (from-to)59-65
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume87
Issue number1
DOIs
StatePublished - Mar 15 1979

Fingerprint

Ethyldimethylaminopropyl Carbodiimide
Carbodiimides
Phosphopyruvate Hydratase
Iodides
Yeast
Catalytic Domain
Yeasts
Water
Enzymes
1-ethyl-3-(4-azonia-4,4-dimethylpentyl)carbodiimide
N-cyclohexyl-N'-2-morpholinoethyl-carbodiimide-methyl-4-toluolsulfonate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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abstract = "Yeast enolase (EC 4.2.1.11) is rapidly inactivated at pH 6.1 by three different water-soluble carbodiimides - 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide hydrochloride, 1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluenesulfonate, and 1-ethyl-3-(4-azonia-4,4-dimethylpentyl)-carbodiimide iodide. Inactivation is most likely due to the modification of essential carboxyl residues at the enzyme active site.",
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Essential carboxyl residues in yeast enolase. / George, Alfred L.; Borders, C. L.

In: Biochemical and Biophysical Research Communications, Vol. 87, No. 1, 15.03.1979, p. 59-65.

Research output: Contribution to journalArticle

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AU - Borders, C. L.

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