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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Glycylpeptide N-tetradecanoyltransferase
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| http://www.biopax.org/relea... |
NMT_YEAST
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
2.3.1.97,
Cell division control protein 72,
Myristoyl-CoA:protein N-myristoyltransferase,
NMT,
Peptide N-myristoyltransferase
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| http://www.biopax.org/relea... |
FUNCTION: Adds 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. CATALYTIC ACTIVITY: Tetradecanoyl-CoA + glycylpeptide = CoA + N- tetradecanoylglycylpeptide. ENZYME REGULATION: Inhibited 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. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for myristoyl-CoA; pH dependence: Optimum pH is 7.5-8.0; SUBUNIT: Monomer. SUBCELLULAR LOCATION: Cytoplasm. PTM: The N-terminus is blocked. MISCELLANEOUS: Has 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. SIMILARITY: Belongs to the NMT family. GENE SYNONYMS: CDC72. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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