Skip Navigation

Cardiovascular Research 1999 43(3):521-531; doi:10.1016/S0008-6363(99)00115-7
© 1999 by European Society of Cardiology
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Andrew, P. J
Right arrow Articles by Mayer, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Andrew, P. J
Right arrow Articles by Mayer, B.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Copyright © 1999, European Society of Cardiology

Enzymatic function of nitric oxide synthases

Penelope J Andrew and Bernd Mayer*

Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Universitätsplatz 2, Graz A-8010, Austria

* Corresponding author. Tel.: +43-316-3805567; fax: +43-316-3809890 mayer{at}kfunigraz.ac.at

Nitric oxide (NO) is synthesised from L-arginine by the enzyme NO synthase (NOS). The complex reaction involves the transfer of electrons from NADPH, via the flavins FAD and FMN in the carboxy-terminal reductase domain, to the haem in the amino-terminal oxygenase domain, where the substrate L-arginine is oxidised to L-citrulline and NO. The haem is essential for dimerisation as well as NO production. The pteridine tetrahydrobiopterin (BH4) is a key feature of NOS, affecting dimerisation and electron transfer, although its full role in catalysis remains to be determined. NOS can also catalyse superoxide anion production, depending on substrate and cofactor availability. There are three main isoforms of the enzyme, named neuronal NOS (nNOS), inducible NOS (iNOS), and endothelial NOS (eNOS), which differ in their dependence on Ca2+, as well as in their expression and activities. These unique features give rise to the distinct subcellular localisations and mechanistic features which are responsible for the physiological and pathophysiological roles of each isoform.

KEYWORDS Nitric oxide; Free radicals; Endothelial function; Endothelial factors; Vasoconstriction/dilation


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Pharmacol. Rev.Home page
N. Toda, K. Ayajiki, and T. Okamura
Cerebral Blood Flow Regulation by Nitric Oxide: Recent Advances
Pharmacol. Rev., March 1, 2009; 61(1): 62 - 97.
[Abstract] [Full Text] [PDF]

Home page
 Circ. Res.Home page
Z. Chen, I-C. Peng, W. Sun, M.-I Su, P.-H. Hsu, Y. Fu, Y. Zhu, K. DeFea, S. Pan, M.-D. Tsai, et al.
AMP-Activated Protein Kinase Functionally Phosphorylates Endothelial Nitric Oxide Synthase Ser633
Circ. Res., February 27, 2009; 104(4): 496 - 505.
[Abstract] [Full Text] [PDF]

Home page
 JPEN J Parenter Enteral NutrHome page
M. C. Richir, R. H. Bouwman, T. Teerlink, M. P.C. Siroen, T. P.G.M. de Vries, and P. A.M. van Leeuwen
The Prominent Role of the Liver in the Elimination of Asymmetric Dimethylarginine (ADMA) and the Consequences of Impaired Hepatic Function
JPEN J Parenter Enteral Nutr, November 1, 2008; 32(6): 613 - 621.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
M. d. C. P. Franco, Z. B. Fortes, E. H. Akamine, E. M. Kawamoto, C. Scavone, L. R. G. de Britto, M. N. Muscara, S. A. Teixeira, R. C. A. Tostes, M. H. C. Carvalho, et al.
Tetrahydrobiopterin improves endothelial dysfunction and vascular oxidative stress in microvessels of intrauterine undernourished rats
J. Physiol., July 1, 2004; 558(1): 239 - 248.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.