N-myristoylation of GAG polyprotein by NMT2

Stable Identifier
R-HSA-184392
Type
Reaction [transition]
Species
Homo sapiens
Related Species
Human immunodeficiency virus 1
Compartment
cytosol
ReviewStatus
5/5
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N-myristoylation of GAG polyprotein by NMT2
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The amino terminal glycine residue of HIV-1 Gag polyprotein is myristoylated (Henderson et al. 1992). Myristoylation of newly synthesized Gag occurs in the cytosol of the infected host cell, with myristoyl-CoA as the myristate donor and the host cell NMT2 enzyme as the catalyst. Human cells express two isoforms of N-myristoyl transferase (NMT) (Giang and Cravatt 1998). The argumant that the second isoform catalyzes this reaction is indirect, based on the the observations that a stable enzyme:substrate complex forms transiently during the reaction (Farazi et al. 2001), and that Gag polyprotein can be found complexed with NMT2 (but not NMT1) in HIV-1-infected human cells (Hill and Skowronski 2005).
Literature References
PubMed ID Title Journal Year
15613341 Human N-myristoyltransferases form stable complexes with lentiviral nef and other viral and cellular substrate proteins

Skowronski, J, Hill, BT

J Virol 2005
11527981 The biology and enzymology of protein N-myristoylation

Gordon, JI, Waksman, G, Farazi, TA

J Biol Chem 2001
9506952 A second mammalian N-myristoyltransferase

Cravatt, BF, Giang, DK

J Biol Chem 1998
Participants
Input
Output
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as an event of
Catalyst Activity

glycylpeptide N-tetradecanoyltransferase activity of NMT2 [cytosol]

Physical Entity
NMT2 [cytosol] (Homo sapiens)
Activity
glycylpeptide N-tetradecanoyltransferase activity (GO:0004379)
Disease
Name Identifier Synonyms
Human immunodeficiency virus infectious disease DOID:526 HIV infection
Authored
Gillespie, ME  (2013-03-07)
Reviewed
Dube, M  (2013-05-21)
Created
D'Eustachio, P  (2006-07-27)
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