Intrinsic and extrinsic modulation of nitric oxide synthase activity

Linda J. Roman; Pavel Martásek; Bettie Sue Siler Masters

doi:10.1021/cr000661e

Intrinsic and extrinsic modulation of nitric oxide synthase activity

Linda J. Roman, Pavel Martásek, Bettie Sue Siler Masters

Biochemistry & Structural Biology

Research output: Contribution to journal › Article › peer-review

172 Scopus citations

Abstract

The NOS isoforms are modulated by a precise symphony of both intrinsic and extrinsic factors. The overall rate of NO production by each of the isoforms is finely tuned by an amazingly complex combination of intrinsic factors, including the heme environment, and dimerization state, CaM binding, the autoinhibitory domain, and the C-terminal tail region, and extrinsic factors, such as posttranslational modifications, phosphorylation, and specific interactions with other proteins.

Original language	English (US)
Pages (from-to)	1179-1189
Number of pages	11
Journal	Chemical Reviews
Volume	102
Issue number	4
DOIs	https://doi.org/10.1021/cr000661e
State	Published - Apr 2002

ASJC Scopus subject areas

Chemistry(all)

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10.1021/cr000661e

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title = "Intrinsic and extrinsic modulation of nitric oxide synthase activity",

abstract = "The NOS isoforms are modulated by a precise symphony of both intrinsic and extrinsic factors. The overall rate of NO production by each of the isoforms is finely tuned by an amazingly complex combination of intrinsic factors, including the heme environment, and dimerization state, CaM binding, the autoinhibitory domain, and the C-terminal tail region, and extrinsic factors, such as posttranslational modifications, phosphorylation, and specific interactions with other proteins.",

author = "Roman, {Linda J.} and Pavel Mart{\'a}sek and Masters, {Bettie Sue Siler}",

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AB - The NOS isoforms are modulated by a precise symphony of both intrinsic and extrinsic factors. The overall rate of NO production by each of the isoforms is finely tuned by an amazingly complex combination of intrinsic factors, including the heme environment, and dimerization state, CaM binding, the autoinhibitory domain, and the C-terminal tail region, and extrinsic factors, such as posttranslational modifications, phosphorylation, and specific interactions with other proteins.

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Intrinsic and extrinsic modulation of nitric oxide synthase activity

Abstract

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