CHEBI:140657 - N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine residue
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This entity has been annotated by a third party. If you would like more
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S(C[C@@H](C(*)=O)NC(*)=O)C[C@H](OC(*)=O)COC(=O)* |
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Outgoing
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N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine residue
(CHEBI:140657)
has functional parent
L-cysteine residue
(CHEBI:29950)
N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine residue
(CHEBI:140657)
is a
organic molecular entity
(CHEBI:50860)
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N-acyl-(S-1,2-diacyl-sn-glyceryl)-L-cysteine residue
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UniProt
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a-mature-triacylated-lipoprotein
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MetaCyc accession
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View more database links |
Hillmann F, Argentini M, Buddelmeijer N (2011) Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase. The Journal of biological chemistry 286, 27936-27946 (Source: SUBMITTER) [PubMed:21676878] [show Abstract] The enzyme apolipoprotein N-acyltransferase (Lnt) is an integral membrane protein that catalyzes the last step in the post-translational modification of bacterial lipoproteins. Lnt undergoes covalent modification in the presence of phospholipids resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the α-amino group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. To gain insight into the catalytic mechanism of this two-step reaction, we overproduced and purified the enzyme of Escherichia coli and studied its N-acyltransferase activity using a novel in vitro assay. The purified enzyme was fully active, as judged by its ability to form a stable thioester acyl-enzyme intermediate and N-acylate the apo-form of the murein lipoprotein Lpp in vitro. Incorporation of [(3)H]palmitate and mass spectrometry analysis demonstrated that Lnt recognized the synthetic diacylglyceryl-modified lipopeptide FSL-1 as a substrate in a mixed micelle assay. Kinetics of Lnt using phosphatidylethanolamine as an acyl donor and FSL-1 as a substrate were consistent with a ping-pong type mechanism, demonstrating slow acyl-enzyme intermediate formation and rapid N-acyl transfer to the apolipopeptide in vitro. In contrast to earlier in vitro observations, the N-acyltransferase activity was strongly affected by the phospholipid headgroup and acyl chain composition. |
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