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
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General
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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
11527981 The biology and enzymology of protein N-myristoylation

Farazi, TA, Waksman, G, Gordon, JI

J Biol Chem 2001
15613341 Human N-myristoyltransferases form stable complexes with lentiviral nef and other viral and cellular substrate proteins

Hill, BT, Skowronski, J

J Virol 2005
9506952 A second mammalian N-myristoyltransferase

Giang, DK, Cravatt, BF

J Biol Chem 1998
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
glycylpeptide N-tetradecanoyltransferase activity of NMT2 [cytosol]
Physical Entity
Activity
Disease
Name Identifier Synonyms
Human immunodeficiency virus infectious disease 526 HIV infection
Authored
Reviewed
Created
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