N-myristoylation of eNOS

Stable Identifier
R-HSA-203611
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
Synonyms
N-terminal glycyl-(protein) + tetradecanoyl-CoA => CoA + H(+) + N-tetradecanoylglycyl-(protein)
ReviewStatus
5/5
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N-myristoylation of eNOS
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The enzymes glycylpeptide N-tetradecanoyltransferase 1 and 2 (NMT1/2) are inferred to mediate the transfer of a myristoyl (MYS) group from myristoyl-CoA to the glycine (Gly) residue exposed by removal of the aminoterminal methionine residue of nascent NOS3 (eNOS, Nitric oxide synthase 3) (Liu & Sessa 1994). The ability of NMT1/2 to mediate N-myristoylation of a wide array of proteins is well established (Gordon et al. 1991), although their activity on NMT1/2 has not been studied.
Literature References
PubMed ID Title Journal Year
2026581 Protein N-myristoylation

Gordon, JI, Duronio, RJ, Rudnick, DA, Adams, SP, Gokel, GW

J Biol Chem 1991
7512951 Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase

Liu, J, Sessa, WC

J Biol Chem 1994
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Catalyst Activity

glycylpeptide N-tetradecanoyltransferase activity of NMT1/2 [cytosol]

Physical Entity
NMT1/2 [cytosol] (Homo sapiens)
Activity
glycylpeptide N-tetradecanoyltransferase activity (GO:0004379)
Inferred From
NMT1/2 transfer MYS to GNAT1 (Homo sapiens)
Cross References
RHEA
Authored
Hemish, J  (2007-10-19)
Reviewed
Enikolopov, G  (2008-02-28)
Hill, DP  (2024-08-02)
Created
Hemish, J  (2007-10-19)
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