Enzyme

Download
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;

3D structure

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.

References

External Links

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:

2.3.1.191;

Phylogenetic Tree:

2.3.1.191;

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

References

TitleAuthorsDatePubMed ID
Defective biosynthesis of the lipid A component of temperature-sensitive firA (omsA) mutant of Escherichia coli.Helander IM, Lindner B, Seydel U, Vaara M1993 Mar 18444173
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 MS1993 Sep 158366125
Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis.Bartling CM, Raetz CR2009 Sep 1519655786
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 RP2008 Jul18456814
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.Bartling CM, Raetz CR2008 May 1318422345
Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis.Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN2007 Mar 1317360522
A continuous fluorescent enzyme assay for early steps of lipid A biosynthesis.Jenkins RJ, Dotson GD2012 Jun 122381368