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Literature summary for 2.3.1.97 extracted from

  • Farazi, T.A.; Manchester, J.K.; Waksman, G.; Gordon, J.I.
    Pre-steady-state kinetic studies of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase mutants identify residues involved in catalysis (2001), Biochemistry, 40, 9177-9186.
    View publication on PubMed
Search for more literature for 2.3.1.97

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutants in Escherichia coli Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E167Q site-directed mutagenesis, kinetics similar to wild-type Saccharomyces cerevisiae
F170A/L171A site-directed mutagenesis, increased Ki for S-(2-oxo)-pentadecyl-CoA, increased Km for peptide substrate, altered enzyme conformation which modifies myristoyl-CoA polarization during catalytic reaction Saccharomyces cerevisiae
additional information C-terminal deletion mutants M454 and L455 produce a 300-400fold reduction in the chemical transformation rate, shift of the rate-limite of the process steps Saccharomyces cerevisiae
N169L site-directed mutagenesis, slightly increased Km for peptide substrate, altered kinetics Saccharomyces cerevisiae
N169L/T205A site-directed mutagenesis, increased Km for peptide substrate, altered kinetics Saccharomyces cerevisiae
T205A site-directed mutagenesis, altered kinetics Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0009
-
 Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val
-
 Saccharomyces cerevisiae
0.0014
-
 myristoyl-CoA
-
 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 gene nmt1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutants from Escherichia coli Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] ordered bi bi mechanism Saccharomyces cerevisiae
a
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] kinetic analysis Saccharomyces cerevisiae
a
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
myristoyl-CoA + Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val
-
 Saccharomyces cerevisiae N-myristoyl-Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val + CoA
-
 ?
myristoyl-CoA + glycylpeptide
-
 Saccharomyces cerevisiae N-myristoylglycylpeptide + CoA
-
 ?

Synonyms

Synonyms Comment Organism
More enzyme belongs to the superfamily of GCN5-related N-acetyltransferases Saccharomyces cerevisiae
Nmt1p
-
 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
 assay at Saccharomyces cerevisiae