LMPD Database

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LMP007135

UniProt Annotations

Entry Information
Gene Nameglycylpeptide N-tetradecanoyltransferase NMT1
Protein EntryNMT_YEAST
UniProt IDP14743
SpeciesYeast (S288c)
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=1.4 uM for myristoyl-CoA {ECO:0000269|PubMed:11478885, ECO:0000269|PubMed:3106975}; pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:11478885, ECO:0000269|PubMed:3106975};
Biophysicochemical PropertiesKinetic parameters: KM=1.4 uM for myristoyl-CoA {ECO:0000269|PubMed:11478885, ECO:0000269|PubMed:3106975}; pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:11478885, ECO:0000269|PubMed:3106975};
Catalytic ActivityTetradecanoyl-CoA + glycylpeptide = CoA + N- tetradecanoylglycylpeptide.
Enzyme RegulationInhibited by diethylpyrocarbonate. Competitively inhibited by S-(2-oxo)pentadecyl-CoA, a non hydrolysable myristoyl-CoA analog, and by SC-58272, a peptidomimetic derived from the N-terminal sequence of a natural substrate.
FunctionAdds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N- terminal glycine in the nascent polypeptide substrates. Uncharged amino acids are preferred at position 2 while neutral residues are favored at positions 3 and 4. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6.
MiscellaneousHas an ordered Bi-Bi kinetic mechanism, with myristoyl-CoA binding taking place prior to peptide binding and CoA release occurring before acylated peptide release. Cooperative interactions between the acyl-CoA and peptide binding sites of NMT contribute to its extraordinary chain-length specificity.
PtmThe N-terminus is blocked.
SimilarityBelongs to the NMT family
SimilarityBelongs to the NMT family. {ECO:0000305}.
Subcellular LocationCytoplasm .
Subcellular LocationCytoplasm {ECO:0000269|PubMed:14562095}.
SubunitMonomer. {ECO:0000269|PubMed:11371195, ECO:0000269|PubMed:9846880}.