| EC Tree |
| 2. Transferases |
| 2.3 Acyltransferases |
| 2.3.1 Transferring groups other than aminoacyl groups |
| ID: | 2.3.1.191 |
|---|---|
| Description: | UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase. |
| Alternative Name: |
UDP-3-O-acyl-glucosamine N-acyltransferase. UDP-3-O-(3-hydroxymyristoyl)-D-glucosamine N-acyltransferase. |
| Cath: | 1.20.5.1620; 3.40.1390.10; 2.160.10.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 2.3.1.191 |
| BRENDA Enzyme Link: | BRENDA 2.3.1.191 |
| KEGG Enzyme Link: | KEGG2.3.1.191 |
| BioCyc Enzyme Link: | BioCyc 2.3.1.191 |
| ExPASy Enzyme Link: | ExPASy2.3.1.191 |
| EC2PDB Enzyme Link: | EC2PDB 2.3.1.191 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.3.1.191 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.3.1.191 |
| IntEnz Enzyme Link: | IntEnz 2.3.1.191 |
| MEDLINE Enzyme Link: | MEDLINE 2.3.1.191 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:17817 | (3R)-hydroxytetradecanoyl-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + holo-[ACP] + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine |
| RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]-[S;H0;+0:4]-[C;H0;+0:5](=[*:6])-[*:7]>>[*:1]-[NH;+0:2]-[C;H0;+0:5](=[*:6])-[*:7].[*:3]-[SH;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Defective biosynthesis of the lipid A component of temperature-sensitive firA (omsA) mutant of Escherichia coli. | Helander IM, Lindner B, Seydel U, Vaara M | 1993 Mar 1 | 8444173 |
| The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis. | Kelly TM, Stachula SA, Raetz CR, Anderson MS | 1993 Sep 15 | 8366125 |
| Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis. | Bartling CM, Raetz CR | 2009 Sep 15 | 19655786 |
| Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. | Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP | 2008 Jul | 18456814 |
| Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis. | Bartling CM, Raetz CR | 2008 May 13 | 18422345 |
| Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis. | Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN | 2007 Mar 13 | 17360522 |
| A continuous fluorescent enzyme assay for early steps of lipid A biosynthesis. | Jenkins RJ, Dotson GD | 2012 Jun 1 | 22381368 |