EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.97 | expression of wild-type and mutants in Escherichia coli | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.97 | E167Q | site-directed mutagenesis, kinetics similar to wild-type | Saccharomyces cerevisiae |
2.3.1.97 | 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 |
2.3.1.97 | 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 |
2.3.1.97 | N169L | site-directed mutagenesis, slightly increased Km for peptide substrate, altered kinetics | Saccharomyces cerevisiae |
2.3.1.97 | N169L/T205A | site-directed mutagenesis, increased Km for peptide substrate, altered kinetics | Saccharomyces cerevisiae |
2.3.1.97 | T205A | site-directed mutagenesis, altered kinetics | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.97 | 0.0009 | - |
Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val | - |
Saccharomyces cerevisiae | |
2.3.1.97 | 0.0014 | - |
myristoyl-CoA | - |
Saccharomyces cerevisiae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.97 | Saccharomyces cerevisiae | - |
gene nmt1 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.97 | recombinant wild-type and mutants from Escherichia coli | Saccharomyces cerevisiae |
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] | ordered bi bi mechanism | Saccharomyces cerevisiae | |
2.3.1.97 | tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] | kinetic analysis | Saccharomyces cerevisiae | |
2.3.1.97 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.97 | myristoyl-CoA + Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val | - |
Saccharomyces cerevisiae | N-myristoyl-Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val + CoA | - |
? | |
2.3.1.97 | myristoyl-CoA + glycylpeptide | - |
Saccharomyces cerevisiae | N-myristoylglycylpeptide + CoA | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.97 | More | enzyme belongs to the superfamily of GCN5-related N-acetyltransferases | Saccharomyces cerevisiae |
2.3.1.97 | Nmt1p | - |
Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.97 | 7.7 | - |
assay at | Saccharomyces cerevisiae |