Literature summary for 2.3.1.97 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

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Application

Application	Comment	Organism
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)

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

Organism

Organism	UniProt	Comment	Textmining
Candida albicans	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	ir

Synonyms

Synonyms	Comment	Organism
N-myristoyl transferase	-	Candida albicans
NMT	-	Candida albicans

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Release 2023.1 (January 2023)