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The H159A mutant of yeast enolase 1 has significant activity.

Abstract：

:The function of His159 in the enolase mechanism is disputed. Recently, Vinarov and Nowak (Biochemistry (1999) 38, 12138-12149) prepared the H159A mutant of yeast enolase 1 and expressed this in Escherichia coli. They reported minimal (ca. 0.01% of the native value) activity, though the protein appeared to be correctly folded, according to its CD spectrum, tryptophan fluorescence, and binding of metal ion and substrate. We prepared H159A enolase using a multicopy plasmid and expressed the enzyme in yeast. Our preparations of H159A enolase have 0.2-0.4% of the native activity under standard assay conditions and are further activated by Mg(2+) concentrations above 1 mM to 1-1.5% of the native activity. Native enolase 1 (and enolase 2) are inhibited by such Mg(2+) concentrations. It is possible that His159 is necessary for correct folding of the enzyme and that expression in E. coli leads to largely misfolded protein.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Brewer JM,Holland MJ,Lebioda L

doi

10.1006/bbrc.2000.3618

subject

Has Abstract

pub_date

2000-10-05 00:00:00

pages

1199-202

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)93618-0

journal_volume

276

pub_type

杂志文章

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