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
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
Search PMC articles PubMed articles NCBI proteins

NMT, N-terminal
Identifiers
Symbol	NMT
Pfam	PF01233
InterPro	IPR022676
CATH	3IU1
SCOP2	3IU1 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

NMT, C-terminal
Identifiers
Symbol	NMT_C
Pfam	PF02799
InterPro	IPR022677
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, a glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) is an enzyme that catalyzes the chemical reaction

tetradecanoyl-CoA + glycylpeptide ${\displaystyle \rightleftharpoons }$ 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

1. 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.
2. 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.
3. 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.