| EC |
2.3.1.269 |
| Accepted name: |
apolipoprotein N-acyltransferase |
| Reaction: |
a phosphoglycerolipid + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine = a 1-lyso-phosphoglycerolipid + a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine |
| Other name(s): |
lnt (gene name); Lnt |
| Systematic name: |
phosphoglyceride:[apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine N-acyltransferase |
| Comments: |
This bacterial enzyme transfers a fatty acid from a membrane phospholipid to form an amide linkage with the N-terminal cysteine residue of apolipoproteins, generating a triacylated molecule. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Gupta, S.D. and Wu, H.C. Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli. FEMS Microbiol. Lett. 62 (1991) 37–41. [PMID: 2032623] |
| 2. |
Robichon, C., Vidal-Ingigliardi, D. and Pugsley, A.P. Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. J. Biol. Chem. 280 (2005) 974–983. [PMID: 15513925] |
| 3. |
Hillmann, F., Argentini, M. and Buddelmeijer, N. Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase. J. Biol. Chem. 286 (2011) 27936–27946. [DOI] [PMID: 21676878] |
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| [EC 2.3.1.269 created 2018] |
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