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In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7.

Abstract：

:This report describes the in vivo phosphorylation of isocitrate lyase and examines the possible consequences to the control of the Kreb's cycle and glyoxylate bypass. NADP-specific isocitrate dehydrogenase from E. coli was the first bacterial protein whose enzymic activity was shown to be modulated by reversible phosphorylation. This enzyme has been thought to be solely responsible for the partitioning of isocitrate between the Kreb's cycle and glyoxylate bypass. No studies to date have examined the possible role of isocitrate lyase in controlling this flux.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Hoyt JC,Reeves HC

doi

10.1016/s0006-291x(88)81177-x

subject

Has Abstract

pub_date

1988-06-16 00:00:00

pages

875-80

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)81177-X

journal_volume

153

pub_type

杂志文章

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