STRUCTURE-FUNCTION ASPECTS IN THE NITRIC OXIDE SYNTHASES

Annual Review of Pharmacology and Toxicology - Tập 37 Số 1 - Trang 339-359 - 1997
Dennis J. Stuehr1,2
1Department of Immunology, The Cleveland Clinic, Cleveland, Ohio 44195
2Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106

Tóm tắt

▪ Abstract  Research on the biological roles of nitric oxide has revealed that it functions as an important signal and effector molecule in a variety of physiologic and pathologic settings. In animals, nitric oxide is synthesized enzymatically from l-arginine through the actions of the nitric oxide synthases (NOSs). The three known NOS isoforms are all dimeric, bi-domain enzymes that contain iron protoporphyrin IX, flavin adenine dinucleotide, flavin mononucleotide, and tetrahydrobiopterin as bound prosthetic groups. This chapter summarizes information regarding the structure-function aspects of the NOSs, which includes composition of the domains, the protein residues and regions involved in prosthetic group binding, catalytic properties of the domains, the relationship between dimeric structure and prosthetic group binding and function, and factors that control assembly of NOS in cells. A general model for NOS structure and assembly is presented.

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Annual Review of Pharmacology and Toxicology

Tập 37 Số 1

339-359

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