Literature summary extracted from

Rudnick, D.A.; McWherter, C.A.; Rocaque, W.J.; Lennon, P.J.; Getman, D.P.; Gordon, J.I.
Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase (1991), J. Biol. Chem., 266, 9732-9739.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.3.1.97	expression in Escherichia coli	Saccharomyces cerevisiae

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.3.1.97	CoA	noncompetitive	Saccharomyces cerevisiae
2.3.1.97	S-(2-Oxo)-pentadecyl-CoA	-	Saccharomyces cerevisiae

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.3.1.97	Saccharomyces cerevisiae	-	gene nmt1	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
2.3.1.97	recombinant from Escherichia coli	Saccharomyces cerevisiae

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.3.1.97	tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]	mechanism	Saccharomyces cerevisiae	a

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.3.1.97	0.15	-	purified recombinant enzyme	Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.3.1.97	myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg	-	Saccharomyces cerevisiae	N-myristoyl-Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg + CoA	-	?
2.3.1.97	myristoyl-CoA + glycylpeptide	-	Saccharomyces cerevisiae	N-myristoylglycylpeptide + CoA	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
2.3.1.97	NMT	-	Saccharomyces cerevisiae

Ki Value [mM]

EC Number	Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
2.3.1.97	0.001	0.0014	S-(2-Oxo)-pentadecyl-CoA	-	Saccharomyces cerevisiae
2.3.1.97	0.275	-	CoA	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)