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EC
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1.14.99.31
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| Transferred entry: | myristoyl-CoA 11-(E) desaturase. Now classified as EC 1.14.19.24, myristoyl-CoA 11-(E) desaturase
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| [EC 1.14.99.31 created 2000, deleted 2015] |
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EC
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1.14.99.32
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| Transferred entry: | myristoyl-CoA 11-(Z) desaturase. Now classified as EC 1.14.19.5, acyl-CoA 11-(Z)-desaturase.
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| [EC 1.14.99.32 created 2000, deleted 2015] |
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| EC |
2.3.1.97 |
| Accepted name: |
glycylpeptide N-tetradecanoyltransferase |
| Reaction: |
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] |
| Glossary: |
tetradecanoyl-CoA = myristoyl-CoA |
| Other name(s): |
NMT (gene name); peptide N-myristoyltransferase; myristoyl-CoA-protein N-myristoyltransferase; myristoyl-coenzyme A:protein N-myristoyl transferase; myristoylating enzymes; protein N-myristoyltransferase; tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase |
| Systematic name: |
tetradecanoyl-CoA:N-terminal-glycine-[protein] N-tetradecanoyltransferase |
| Comments: |
The enzyme catalyses the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 110071-61-9 |
| References: |
| 1. |
Guertin, D., Gris-Miron, L. and Riendeau, D. Identification of a 51-kilodalton polypeptide fatty acyl chain acceptor in soluble extracts from mouse cardiac tissue. Biochem. Cell Biol. 64 (1986) 1249–1255. [PMID: 3566958] |
| 2. |
Heuckeroth, R.O., Towler, D.A., Adams, S.P., Glaser, L. and Gordon, J.I. 11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase. J. Biol. Chem. 263 (1988) 2127–2133. [PMID: 3123489] |
| 3. |
Towler, D.A., Adams, S.P., Eubanks, S.R., Towery, D.S., Jackson-Machelski, E., Glaser, L. and Gordon, J.I. Purification and characterization of yeast myristoyl CoA:protein N-myristoyltransferase. Proc. Natl. Acad. Sci. USA 84 (1987) 2708–2712. [PMID: 3106975] |
| 4. |
McIlhinney, R.A., Young, K., Egerton, M., Camble, R., White, A. and Soloviev, M. Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme. Biochem. J. 333 (1998) 491–495. [PMID: 9677304] |
| 5. |
Farazi, T.A., Waksman, G. and Gordon, J.I. Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis. Biochemistry 40 (2001) 6335–6343. [PMID: 11371195] |
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| [EC 2.3.1.97 created 1989, modified 1990, modified 2018] |
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