EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.191 | - |
Chlamydia trachomatis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.3.1.191 | hanging drop vapor diffusion. Crystallographic analyses of recombinant Chlamydia trachomatis LpxD in complex with UDP-GlcNAc, which represents a fragment of substrate, and fatty acid extracted from the bacterial expression system, apo-structure at 2.7 A resolution, and two structures with bound UDP-N-acetylglucosamine (UDP-GlcNAc) at 2.2 A and 3.1 A resolution | Chlamydia trachomatis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.191 | (3R)-3-hydroxyarachidonoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine | Chlamydia trachomatis | the external layer of the Gram-negative bacterial outer membrane is primarily composed of a protective, selectively permeable lipopolysaccharide. The biosynthesis of lipopolysaccharide relies on UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD), which transfers 3-hydroxy-arachidonic acid from acyl carrier protein to the 2' amine of UDP-3-O-myristoyl glucosamine. CtLpxD is expected to utilize R-3-hydroxyarachidonoyl-[acyl-carrier protein] and UDP-3-O-(myristoyl)-R-D-glucosamine, based on the predominant molecular species of Chlamydia trachomatis lipid A. This proposal is not validated by in vitro assays | UDP-2-N-((3R)-3-hydroxyarachidonoyl)-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein] | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.191 | Chlamydia trachomatis | P0CD76 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.191 | - |
Chlamydia trachomatis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.191 | (3R)-3-hydroxyarachidonoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine | the external layer of the Gram-negative bacterial outer membrane is primarily composed of a protective, selectively permeable lipopolysaccharide. The biosynthesis of lipopolysaccharide relies on UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD), which transfers 3-hydroxy-arachidonic acid from acyl carrier protein to the 2' amine of UDP-3-O-myristoyl glucosamine. CtLpxD is expected to utilize R-3-hydroxyarachidonoyl-[acyl-carrier protein] and UDP-3-O-(myristoyl)-R-D-glucosamine, based on the predominant molecular species of Chlamydia trachomatis lipid A. This proposal is not validated by in vitro assays | Chlamydia trachomatis | UDP-2-N-((3R)-3-hydroxyarachidonoyl)-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein] | - |
? | |
2.3.1.191 | additional information | His247 and His284 contribute to a mechanism involving nucleophilic attack by the amine of one substrate on the carbonyl carbon of an acyl carrier protein thioester conjugate | Chlamydia trachomatis | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.191 | homotrimer | each subunit of which is constructed from a novel combination of an N-terminal uridine binding domain, a core lipid-binding domain, and a C-terminal helical extension. Highly conserved residues dominate nucleotide binding. Phe43 and Tyr49 form pi-stacking interactions with uracil, and Asn46 and His284 form hydrogen bonds with the phosphate groups | Chlamydia trachomatis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.191 | CtLpxD | - |
Chlamydia trachomatis |
2.3.1.191 | UDP-3-O-acyl-glucosamine N-acyltransferase | - |
Chlamydia trachomatis |