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Details on Person The amino terminal glycine residue of HIV-1 Gag polyprotein ...

Class:IdSummation:184363
_displayNameThe amino terminal glycine residue of HIV-1 Gag polyprotein ...
_timestamp2006-07-27 16:06:54
created[InstanceEdit:184440] D'Eustachio, P, 2006-07-27 16:05:42
literatureReference[LiteratureReference:184353] A second mammalian N-myristoyltransferase
[LiteratureReference:184267] Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processings, and complete amino acid sequences
[LiteratureReference:167501] Human N-myristoyltransferases form stable complexes with lentiviral nef and other viral and cellular substrate proteins
[LiteratureReference:184378] The biology and enzymology of protein N-myristoylation
textThe 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).
(summation)[Reaction:184392] N-myristoylation of GAG polyprotein by NMT2 [Homo sapiens]
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