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Endothelial nitric oxide synthase is myristylated
Author(s) -
Pollock Jennifer S.,
Klinghofer Vered,
Förstermann Ulrich,
Murad Ferid
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80816-y
Subject(s) - nitric oxide synthase , nitric oxide , enzyme , biochemistry , chemistry , endothelium , endothelium derived relaxing factor , nitric oxide synthase type iii , biology , endocrinology , organic chemistry , enos
The enzyme responsible for the synthesis of endothelium‐derived relaxing factor and/or nitric oxide in the endothelium has been described as a particulate enzyme, whereas other isoforms of nitric oxide synthase are soluble enzymes. Here we are reporting that endothelial cells metabolically incorporate myristate (C14), but not palmitate (C16), into nitric oxide synthase. We are postulating that the endothelial‐derived nitric oxide synthase is a particulate enzyme because of the fatty acid acylation of the protein which ‘anchors’ the enzyme into the membrane either directly or via another membrane‐bound protein.