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Article

A connecting hinge represses the activity of endothelial nitric oxide synthase.

Proceedings of the National Academy of Sciences of the United States of America - 29 May 2007

Haque Mohammad Mahfuzul, Panda Koustubh, Tejero Jesús, Aulak Kulwant S, Fadlalla Mohammed Adam, Mustovich Anthony T, Stuehr Dennis J

Abstract excerpt

In mammals, endothelial nitric oxide synthase (eNOS) has the weakest activity, being one-tenth and one-sixth as active as the inducible NOS (iNOS) and the neuronal NOS (nNOS), respectively. The basis for this weak activity is unclear. We hypothesized that a hinge element that connects the FMN module in the reductase domain but is shorter and of unique composition in eNOS may be involved. To test this hypothesis,...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17517617
DOI: 10.1073/pnas.0700332104
PMCID: PMC1890481

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