Biology: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 number | 2.3.1.97 | ||||||||
| CAS number | 110071-61-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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 1IIC, 1IID, 1IYK, 1IYL, 1RXT, 2NMT, 2P6E, 2P6F, and 2P6G.
The enzyme folds into two domains, each with a double EF-hand arrangement.
References
- ↑ "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. 1988. 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. PMID 21449552.
- "Identification of a 51-kilodalton polypeptide fatty acyl chain acceptor in soluble extracts from mouse cardiac tissue". Biochem. Cell Biol. 64 (12): 1249–55. 1986. doi:10.1139/o86-164. PMID 3566958.
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