Mutations at lysine 525 of inducible nitric-oxide synthase affect its Ca2+-independent activity

S. J. Lee, K. Beckingham, J. T. Stull

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Calmodulin binding to inducible nitric-oxide synthase may play an important role in its Ca2+-independent activity. Studies of inducible nitric-oxide synthase chimeras containing the calmodulin binding sequence of neuronal or endothelial nitric-oxide synthases show that the calmodulin binding sequence of inducible nitric-oxide synthase is necessary but not sufficient for the Ca2+-independent activity. The mutations at lysine 525 located at the C terminus of the calmodulin binding sequence of inducible nitric-oxide synthase were examined for the effects on the Ca2+-independent activity with chimeras containing the oxygenase or reductase domains of inducible or neuronal nitric-oxide synthases. Results show that the Ca2+-independent binding of calmodulin is not solely responsible for maximal Ca2+-independent activity of inducible nitric-oxide synthase. Lysine 525 of inducible nitric-oxide synthase may also play an important role in coordinating the maximal Ca2+-independent activity.

Original languageEnglish (US)
Pages (from-to)36067-36072
Number of pages6
JournalJournal of Biological Chemistry
Volume275
Issue number46
DOIs
StatePublished - Nov 17 2000

Fingerprint

Nitric Oxide Synthase Type II
Lysine
Calmodulin
Mutation
Oxygenases
Nitric Oxide Synthase Type I
Nitric Oxide Synthase Type III
Oxidoreductases

ASJC Scopus subject areas

  • Biochemistry

Cite this

Mutations at lysine 525 of inducible nitric-oxide synthase affect its Ca2+-independent activity. / Lee, S. J.; Beckingham, K.; Stull, J. T.

In: Journal of Biological Chemistry, Vol. 275, No. 46, 17.11.2000, p. 36067-36072.

Research output: Contribution to journalArticle

@article{e3c99d85b7664ba68bf1a076e20c01f8,
title = "Mutations at lysine 525 of inducible nitric-oxide synthase affect its Ca2+-independent activity",
abstract = "Calmodulin binding to inducible nitric-oxide synthase may play an important role in its Ca2+-independent activity. Studies of inducible nitric-oxide synthase chimeras containing the calmodulin binding sequence of neuronal or endothelial nitric-oxide synthases show that the calmodulin binding sequence of inducible nitric-oxide synthase is necessary but not sufficient for the Ca2+-independent activity. The mutations at lysine 525 located at the C terminus of the calmodulin binding sequence of inducible nitric-oxide synthase were examined for the effects on the Ca2+-independent activity with chimeras containing the oxygenase or reductase domains of inducible or neuronal nitric-oxide synthases. Results show that the Ca2+-independent binding of calmodulin is not solely responsible for maximal Ca2+-independent activity of inducible nitric-oxide synthase. Lysine 525 of inducible nitric-oxide synthase may also play an important role in coordinating the maximal Ca2+-independent activity.",
author = "Lee, {S. J.} and K. Beckingham and Stull, {J. T.}",
year = "2000",
month = "11",
day = "17",
doi = "10.1074/jbc.M003935200",
language = "English (US)",
volume = "275",
pages = "36067--36072",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "46",

}

TY - JOUR

T1 - Mutations at lysine 525 of inducible nitric-oxide synthase affect its Ca2+-independent activity

AU - Lee, S. J.

AU - Beckingham, K.

AU - Stull, J. T.

PY - 2000/11/17

Y1 - 2000/11/17

N2 - Calmodulin binding to inducible nitric-oxide synthase may play an important role in its Ca2+-independent activity. Studies of inducible nitric-oxide synthase chimeras containing the calmodulin binding sequence of neuronal or endothelial nitric-oxide synthases show that the calmodulin binding sequence of inducible nitric-oxide synthase is necessary but not sufficient for the Ca2+-independent activity. The mutations at lysine 525 located at the C terminus of the calmodulin binding sequence of inducible nitric-oxide synthase were examined for the effects on the Ca2+-independent activity with chimeras containing the oxygenase or reductase domains of inducible or neuronal nitric-oxide synthases. Results show that the Ca2+-independent binding of calmodulin is not solely responsible for maximal Ca2+-independent activity of inducible nitric-oxide synthase. Lysine 525 of inducible nitric-oxide synthase may also play an important role in coordinating the maximal Ca2+-independent activity.

AB - Calmodulin binding to inducible nitric-oxide synthase may play an important role in its Ca2+-independent activity. Studies of inducible nitric-oxide synthase chimeras containing the calmodulin binding sequence of neuronal or endothelial nitric-oxide synthases show that the calmodulin binding sequence of inducible nitric-oxide synthase is necessary but not sufficient for the Ca2+-independent activity. The mutations at lysine 525 located at the C terminus of the calmodulin binding sequence of inducible nitric-oxide synthase were examined for the effects on the Ca2+-independent activity with chimeras containing the oxygenase or reductase domains of inducible or neuronal nitric-oxide synthases. Results show that the Ca2+-independent binding of calmodulin is not solely responsible for maximal Ca2+-independent activity of inducible nitric-oxide synthase. Lysine 525 of inducible nitric-oxide synthase may also play an important role in coordinating the maximal Ca2+-independent activity.

UR - http://www.scopus.com/inward/record.url?scp=0034680837&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034680837&partnerID=8YFLogxK

U2 - 10.1074/jbc.M003935200

DO - 10.1074/jbc.M003935200

M3 - Article

VL - 275

SP - 36067

EP - 36072

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 46

ER -