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Literature summary for 2.3.1.269 extracted from

  • Cheng, W.; Doyle, D.A.; El Arnaout, T.
    The N-acyltransferase Lnt structure-function insights from recent simultaneous studies (2018), Int. J. Biol. Macromol., 117, 870-877 .
    View publication on PubMed
Search for more literature for 2.3.1.269

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral membrane protein Escherichia coli 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a phosphoglycerolipid + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine Escherichia coli
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 a 1-lyso-phosphoglycerolipid + a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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 ?
phosphatidylethanolamine + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine Escherichia coli
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 1-lyso-phosphatidylethanolamine + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P23930
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a phosphoglycerolipid + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
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 Escherichia coli a 1-lyso-phosphoglycerolipid + a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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 ?
phosphatidylethanolamine + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
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 Escherichia coli 1-lyso-phosphatidylethanolamine + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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 ?

Synonyms

Synonyms Comment Organism
lnt
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 Escherichia coli

General Information

General Information Comment Organism
evolution apolipoprotein N-acyltransferase Lnt is Lnt is a reverse amidase and belongs to the nitrilase superfamily. Nitrilases generally require the Glu/Lys/Cys catalytic triad's conformation, also found in Lnt, and have a conserved alphabetabetaalpha sandwich fold. First, the intermediate is formed by the nucleophilic attack on the sn-1-glycerophospholipid's carbonyl (in phosphatidylethanolamine (PE), preferentially). Second, the intermediate (acyl-Lnt) undergoes a nucleophilic attack by the alpha-amino group of the protein substrate generating the triacylated lipoprotein Escherichia coli
metabolism three membrane proteins are involved in processing precursors of lipoproteins, in the following order: the diacylglyceryl transferase Lgt, the signal peptidase LspA, and the N-acyltransferase Lnt Escherichia coli
additional information structure-function analysis of enzyme Lnt, significance of unique features in terms of substrate's recognition and binding mechanism influenced by exclusive residues, two transmembrane helices, and a flexible loop, structure comparisons, detailed overview. In the Lnt structure, a catalytic triad (E267/K335/C387) is accessible near TMHs 3, 4 and 5, and a long and unique loop (also described as an arm, lid, etc.) containing a short helix. The Lnt full reaction occurs as a two-step ping-pong. E343 as an important and conserved residue Escherichia coli
physiological function Lnt acts on apolipoproteins. It catalyzes the transfer of an acyl chain from the sn-1 position of a lipid to the N-terminal cysteine, generating a triacylated lipoprotein. In its structure, a catalytic triad (E267/K335/C387) is accessible near TMHs 3, 4 and 5, and a long and unique loop (also described as an arm, lid, etc.) containing a short helix Escherichia coli