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Activation and inactivation of an enzyme catalyzed by a single, bifunctional protein: a new example and why.

Abstract：

:Recent studies have shown that the light-dark mediated regulation of the leaf photosynthetic enzyme pyruvate, Pi dikinase results from interconversion between an active nonphosphorylated form of the enzyme and an inactive form phosphorylated on a threonine residue. These phosphorylation and dephosphorylation reactions are apparently catalyzed by a single protein termed the pyruvate, Pi dikinase regulatory protein and, notably, both reactions are mechanistically unique. We consider the evidence that this regulatory protein belongs to a group of unusual bifunctional enzymes that catalyze opposing reactions, apparently at separate catalytic sites on the same polypeptide. In three of the four known cases these bifunctional enzymes interconvert the active and inactive forms of another enzyme. The possible advantages of such opposing reactions being catalyzed by the same protein are considered.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Burnell JN,Hatch MD

doi

10.1016/0003-9861(86)90219-5

subject

Has Abstract

pub_date

1986-03-01 00:00:00

pages

297-304

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(86)90219-5

journal_volume

245

pub_type

杂志文章,评审

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