Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.3.1.97: glycylpeptide N-tetradecanoyltransferase

This is an abbreviated version!
For detailed information about glycylpeptide N-tetradecanoyltransferase, go to the full flat file.

Word Map on EC 2.3.1.97

Reaction

tetradecanoyl-CoA
+
an N-terminal-glycyl-[protein]
=
CoA
 +
an N-terminal-N-tetradecanoylglycyl-[protein]

Synonyms

CaNMT, cell division control protein 72, dipeptide N-myristoyltransferase 2, glycylpeptide N-tetradecanoyltransferase, glycylpeptide N-tetradecanoyltransferase 1, glycylpeptide N-tetradecanoyltransferase 2, HsNMT1, HsNMT2, LmNMT, More, myristoyl-CoA-protein N-myristoyltransferase, myristoyl-CoA: protein N-myristoyltransferase, myristoyl-CoA:protein N-myristoyltransferase, myristoyl-CoA:protein N-myristoyltransferase 1, myristoyl-CoA:protein N-myristoyltransferase 2, myristoyl-CoA:protein N-myristoyltransferase type 2, myristoyl-coenzyme A:protein N-myristoyl transferase, myristoyl-coenzyme A:protein N-myristoyltransferase, myristoylating enzymes, myristoyltransferase, myristoyltransferase type 1, myristoyltransferase, protein N-, N-myristoyl transferase, N-myristoyltransferase, N-myristoyltransferase 1, N-myristoyltransferase 2, NMT, NMT 1, NMT 2, NMT-1, NMT-2, NMT1, Nmt1p, NMT2, peptide N-myristoyltransferase, peptide N-myristoyltransferase 1, peptide N-myristoyltransferase 2, protein N-myristoyltransferase, PVX_085815, TbNMT, type I N-myristoyltransferase, type II N-myristoyltransferase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.97 glycylpeptide N-tetradecanoyltransferase

Crystallization

Crystallization on EC 2.3.1.97 - glycylpeptide N-tetradecanoyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitors 2,6-dichloro-4-[2-(4-methylpiperazin-1-yl)pyridin-4-yl]-N-(1,5-dimethyl-3-isobutyl-1H-pyrazol-4-yl)benzenesulfonamide and 2,6-dichloro-4-[2-(4-methylpiperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide binding in the peptide substrate pocket
ternary complex of NMT with S-(2-oxo)pentadecyl-CoA, a myristoyl-CoA analogue cofactor, and synthetic inhibitor Ro-09-4879, 3-[[3-methyl-2-[[2,3,4-tris(fluoranyl)phenoxy]methyl]-1-benzofuran-4-yl]oxy]-N-(pyridin-3-ylmethyl)propan-1-amine, to a resolution of 2.1 A
comparative binding site analysis and molecular docking studies of Leishmania major and Candida albicans NMT and molecular docking studies with benzoheterocyclic analogues
ternary complex formation incubation of protein, 60 mg/ml, with 5fold molar of myristoyl-CoA and inhibitor SC-58272 for a few hours, hanging drop at 4°C, from 0.2 M ammonium acetate, 50 mM HEPES, pH 7.5, 10-12% polyethylene glycol 3350, 2-3 weeks, crystal structure determination by X-ray diffraction analysis
-
NMT1 structures in complex with reactive cognate lipid and peptide substrates
in complex with inhibitor 4-(4-chloro-2-[5-[(trimethyl-1H-pyrazol-4-yl)methyl]-1,3,4-oxadiazol-2-yl]phenoxy)piperidine. The basic piperidine moiety forms a polar interaction with the carboxylate of the C-terminal residue, Leu421 and a water-mediated interaction with Tyr92, mimicking the N-terminus of substrate peptides. In addition, the trimethyl pyrazole substituent forms pi-pi and polar interactions with Phe90 and Ser330, respectively
purified recombinant enzyme in complex with the non-hydrolysable substrate analogue S-(2-oxo)pentadecyl-CoA, X-ray diffraction structure determination and analysis at 1.4 A resolution, molecular replacement method
purified recombinant His-tagged NMT in complex with the non-hydrolysable substrate analogue S-(2-oxo)pentadecyl-CoA, hanging drop vapour diffusion method, mixing of 0.00125 ml of protein solution containing 8 mg/ml protein in 50 mM Tris, pH 8.0, 50 mM NaCl , with 0.00125 l of reservoir solution containing 0.6 M lithium chloride, 20% w/v PEG 6000, 4% v/v 1,4-butanediol in 0.5 M sodium citrate, pH 4.0, equilibration against 0.8 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.4 A resolution, molecular replacement
comparative binding site analysis and molecular docking studies of Leishmania major and Candida albicans NMT and molecular docking studies with benzoheterocyclic analogues
in complex with inhibitors N-[5-[(4R)-1-[(3R)-3-amino-4-(4-chlorophenyl)butanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]-2-chlorophenyl]-2-(4-fluorophenyl)acetamide and N-[2-chloro-5-[(3S,4R)-1-[4-(4-chlorophenyl)-3-hydroxybutanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]phenyl]-2-(4-fluorophenyl)acetamide. The para-fluorophenyl acetamide in ortho-position to the chlorine atom in compound N-[5-[(4R)-1-[(3R)-3-amino-4-(4-chlorophenyl)butanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]-2-chlorophenyl]-2-(4-fluorophenyl)acetamide significantly improves potency. This could potentially introduce hydrogen bonding between the acetamide carbonyl and Tyr345 and Asn376 and allow the compound to extend into a hydrophobic pocket
in complex with both myristoyl-CoA and inhibitor N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide. The inhibitor sits in the peptide-binding pocket, and mimics the key recognition elements involved in binding the parent peptide
hanging drops over a solution of 0.1 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.4, 20°C, 20% polyethylene glycol 4000, protein 25 mg/ml, a few days, structure determination and analysis by X-ray diffraction of binary and ternary complexes of enzyme, peptide substrate or myristoyl-CoA and inhibitor