View source for Glycylpeptide N-tetradecanoyltransferase

{{infobox enzyme
| Name       = glycylpeptide N-tetradecanoyltransferase
| EC_number  = 2.3.1.97
| CAS_number = 110071-61-9
| GO_code    = 0004379
| image      = File:N-Myristoyltransferase Subunit Bound to Myristoyl-CoA.png
| width      =
| caption    = Crystal structure of human type-I N-myristoyltransferase with bound myristoyl-CoA. Myristoyl-CoA (red). PDB ID: 3IU1 
}}
{{Pfam box
|Name=NMT, N-terminal
|Symbol=NMT
|Pfam=PF01233
|InterPro=IPR022676
|CATH=3IU1
|SCOP=3IU1
}}
{{Pfam box
|Name=NMT, C-terminal
|Symbol=NMT_C
|Pfam=PF02799
|InterPro=IPR022677
}}

In [[enzymology]], a '''glycylpeptide N-tetradecanoyltransferase''' ({{EC number|2.3.1.97}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:tetradecanoyl-CoA + glycylpeptide <math>\rightleftharpoons</math> CoA + N-tetradecanoylglycylpeptide

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[tetradecanoyl-CoA]] and [[glycylpeptide]], whereas its two [[product (chemistry)|products]] are [[coenzyme A|CoA]] and [[N-tetradecanoylglycylpeptide]]. It participates in the N-[[Myristoylation]] of proteins, and in vertebrates there are two isoenzymes [[N-myristoyltransferase 1|NMT1]] and [[NMT2]].

Besides tetradecanoyl-CoA, this enzyme is also capable of using modified versions of this substrate.<ref name=pmid3123489>{{cite journal | vauthors = Heuckeroth RO, Towler DA, Adams SP, Glaser L, Gordon JI | date= 1988 | title = 11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase | journal = J. Biol. Chem. | volume = 263 | pages = 2127&ndash;33 | pmid = 3123489 | issue = 5 | doi= 10.1016/S0021-9258(18)69180-X | doi-access= free }}</ref> 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 activator]]s.<ref>{{cite journal |last1=Rundle |first1=Dana R. |last2=Rajala |first2=Raju V.S. |last3=Anderson |first3=Robert E. |title=Characterization of Type I and Type II Myristoyl-CoA:protein N -Myristoyltransferases with the Acyl-CoAs found on Heterogeneously Acylated Retinal Proteins |journal=Experimental Eye Research |date=July 2002 |volume=75 |issue=1 |pages=87–97 |doi=10.1006/exer.2002.1189|pmid=12123640 }}</ref> This is mainly a result of a special set of fatty-acid-CoA substrates available in the retina.<ref>{{cite journal |last1=Bereta |first1=G |last2=Palczewski |first2=K |title=Heterogeneous N-terminal acylation of retinal proteins results from the retina's unusual lipid metabolism. |journal=Biochemistry |date=10 May 2011 |volume=50 |issue=18 |pages=3764–76 |doi=10.1021/bi200245t |pmid=21449552 |pmc=3086940}}</ref>

==Nomenclature==
This enzyme belongs to the family of [[transferase]]s, specifically those N-[[acyltransferase]]s transferring groups other than aminoacyl groups (cd04301).  The [[List of enzymes|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 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1IIC}}, {{PDB link|1IID}}, {{PDB link|1IYK}}, {{PDB link|1IYL}}, {{PDB link|1RXT}}, {{PDB link|2NMT}}, {{PDB link|2P6E}}, {{PDB link|2P6F}}, and {{PDB link|2P6G}}.

The enzyme folds into two domains, each with a double [[EF-hand]] arrangement.

==References==
{{reflist|33em}}
* {{cite journal | vauthors = Guertin D, Grise-Miron L, Riendeau D | date= 1986 | title = Identification of a 51-kilodalton polypeptide fatty acyl chain acceptor in soluble extracts from mouse cardiac tissue | journal = Biochem. Cell Biol. | volume = 64 | pages = 1249&ndash;55 | pmid = 3566958 | doi = 10.1139/o86-164 | issue = 12 }}

{{Acyltransferases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}

[[Category:EC 2.3.1]]
[[Category:Enzymes of known structure]]


{{2.3-enzyme-stub}}