Enzyme

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EC Tree
     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.269
Description:Apolipoprotein N-acyltransferase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.269
BRENDA Enzyme Link: BRENDA 2.3.1.269
KEGG Enzyme Link: KEGG2.3.1.269
BioCyc Enzyme Link: BioCyc 2.3.1.269
ExPASy Enzyme Link: ExPASy2.3.1.269
EC2PDB Enzyme Link: EC2PDB 2.3.1.269
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.269
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.269
IntEnz Enzyme Link: IntEnz 2.3.1.269
MEDLINE Enzyme Link: MEDLINE 2.3.1.269
MSA:

2.3.1.269;

Phylogenetic Tree:

2.3.1.269;

Uniprot:
M-CSA:
RHEA:48228 [lipoprotein]-N-terminal-S-1,2-diacyl-sn-glyceryl-L-cysteine + a glycerophospholipid = [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine + a 1-lyso-glycerophospholipid + H(+)
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[O;H0;+0:6]-[*:7]>>[*:1]-[NH;+0:2]-[C;H0;+0:4](=[*:3])-[*:5].[*:7]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase.Hillmann F, Argentini M, Buddelmeijer N2011 Aug 1221676878
Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli.Gupta SD, Wu HC1991 Feb2032623
Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli.Robichon C, Vidal-Ingigliardi D, Pugsley AP2005 Jan 1415513925