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Neuronal nitric oxide synthase specific autophosphorylation in baculovirus/Sf9 insect cell system.

Abstract：

:Neuronal nitric oxide synthase (nNOS) is a calmodulin (CaM)-dependent enzyme, which generates the ubiquitous biological mediator nitric oxide. In this study, wild-type or mutant form of rat nNOS was overexpressed in a baculovirus/Sf9 insect cell system and examined for autophosphorylation. Incubation of purified wild-type nNOS in the presence of Mg2+ and ATP result in phosphorylation of nNOS. Deletional mutant of the nNOS amino terminus which contains G-Q-G-A-G-S sequence, however, shows loss of phosphorylation. Furthermore, purified wild-type rat liver cytokine-induced NOS (iNOS), which does not contain G-Q-G-A-G-S sequence, shows no phosphorylation activity. We also found that the ratio of wild-type nNOS phosphorylation was independent of nNOS concentration, consistent with an intramolecular reaction. These data suggest that nNOS-specific autophosphorylation pathway might be involved in the regulation of enzyme activity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Watanabe Y,Terashima K,Hidaka H

doi

10.1006/bbrc.1996.0286

subject

Has Abstract

pub_date

1996-02-15 00:00:00

pages

638-43

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)90286-7

journal_volume

219

pub_type

杂志文章

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