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Literature summary extracted from

  • Heal, W.; Wickramasinghe, S.; Bowyer, P.; Holder, A.; Smith, D.; Leatherbarrow, R.; Tate, E.
    Site-specific N-terminal labelling of proteins in vitro and in vivo using N-myristoyl transferase and bioorthogonal ligation chemistry (2008), Chem. Commun. (Camb. ), 8, 480-482.
No PubMed abstract available

Application

EC Number Application Comment Organism
2.3.1.97 molecular biology the enzyme can be used for protein N-myristoylation as a tag labeling technique in recombinant expresssion systems. CaNMT is an effective tool for in vitro and in vivo transfer of an azide-modified acid to the N-terminus of a polypeptide derived from a species entirely unrelated to Candida albicans Candida albicans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.97 expression in Escherichia coli strain BL21 Candida albicans

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.97 Candida albicans
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.97 tetradecanoyl-CoA + Plasmodium falciparum ADP ribosylation factor 1 peptide model substrate, N-myristoylation of a glycine residue Candida albicans CoA + N-myristoylated Plasmodium falciparum ADP ribosylation factor 1 peptide
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 ir

Synonyms

EC Number Synonyms Comment Organism
2.3.1.97 N-myristoyl transferase
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 Candida albicans
2.3.1.97 NMT
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 Candida albicans