Glycylpeptide N-tetradecanoyltransferase
| glycylpeptide N-tetradecanoyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure of human type-I N-myristoyltransferase with bound myristoyl-CoA. Myristoyl-CoA (red). PDB ID: 3IU1 | |||||||||
| Identifiers | |||||||||
| EC no. | 2.3.1.97 | ||||||||
| CAS no. | 110071-61-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| NMT, N-terminal | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | NMT | ||||||
| Pfam | PF01233 | ||||||
| InterPro | IPR022676 | ||||||
| CATH | 3IU1 | ||||||
| SCOP2 | 3IU1 / SCOPe / SUPFAM | ||||||
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| NMT, C-terminal | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | NMT_C | ||||||
| Pfam | PF02799 | ||||||
| InterPro | IPR022677 | ||||||
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In enzymology, a glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) is an enzyme that catalyzes the chemical reaction
- tetradecanoyl-CoA + glycylpeptide CoA + N-tetradecanoylglycylpeptide
Thus, the two substrates of this enzyme are tetradecanoyl-CoA and glycylpeptide, whereas its two products are CoA and N-tetradecanoylglycylpeptide. It participates in the N-Myristoylation of proteins, and in vertebrates there are two isoenzymes NMT1 and NMT2.
Besides tetradecanoyl-CoA, this enzyme is also capable of using modified versions of this substrate.[1] In human retina, an even wider range of fatty acids, including 14:1 n–9, 14:2n–6, and 12:0, are accepted by the enzyme and grafted onto guanylate cyclase activators.[2] This is mainly a result of a special set of fatty-acid-CoA substrates available in the retina.[3]
Nomenclature
This enzyme belongs to the family of transferases, specifically those N-acyltransferases transferring groups other than aminoacyl groups (cd04301). The systematic name of this enzyme class is tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase. Other names in common use include peptide N-myristoyltransferase (NMT), myristoyl-CoA-protein N-myristoyltransferase, myristoyl-coenzyme A:protein N-myristoyl transferase, myristoylating enzymes, and protein N-myristoyltransferase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1IIC, PDB: 1IID, PDB: 1IYK, PDB: 1IYL, PDB: 1RXT, PDB: 2NMT, PDB: 2P6E, PDB: 2P6F, and PDB: 2P6G.
The enzyme folds into two domains, each with a double EF-hand arrangement.
References
- ↑ Heuckeroth RO, Towler DA, Adams SP, Glaser L, Gordon JI (1988). "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 (5): 2127–33. doi:10.1016/S0021-9258(18)69180-X. PMID 3123489.
- ↑ Rundle, Dana R.; Rajala, Raju V.S.; Anderson, Robert E. (July 2002). "Characterization of Type I and Type II Myristoyl-CoA:protein N -Myristoyltransferases with the Acyl-CoAs found on Heterogeneously Acylated Retinal Proteins". Experimental Eye Research. 75 (1): 87–97. doi:10.1006/exer.2002.1189. PMID 12123640.
- ↑ Bereta, G; Palczewski, K (10 May 2011). "Heterogeneous N-terminal acylation of retinal proteins results from the retina's unusual lipid metabolism". Biochemistry. 50 (18): 3764–76. doi:10.1021/bi200245t. PMC 3086940. PMID 21449552.
- Guertin D, Grise-Miron L, Riendeau D (1986). "Identification of a 51-kilodalton polypeptide fatty acyl chain acceptor in soluble extracts from mouse cardiac tissue". Biochem. Cell Biol. 64 (12): 1249–55. Bibcode:1986BCB....64.1249G. doi:10.1139/o86-164. PMID 3566958.