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Information on EC 2.3.1.191 - UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase and Organism(s) Chlamydia trachomatis and UniProt Accession P0CD76

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IUBMB Comments
The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia coli prefers (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] , but it does not have an absolute specificity for 14-carbon hydroxy fatty acids, as it can transfer other fatty acids, including odd-chain fatty acids, if they are available to the organism .
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Chlamydia trachomatis
UNIPROT: P0CD76
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The taxonomic range for the selected organisms is: Chlamydia trachomatis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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a (3R)-3-hydroxyacyl-[acyl-carrier protein]
+
a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
=
a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
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a holo-[acyl-carrier protein]
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a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
=
a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
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Synonyms
eclpxd, lpxd1, lpxd2, ctlpxd, pa3646, udp-3-o-acyl-glucosamine n-acyltransferase, udp-3-o-(r-3-hydroxyacyl)-glucosamine acyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-3-O-acyl-glucosamine N-acyltransferase
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine N-acyltransferase
The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia coli prefers (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] [3], but it does not have an absolute specificity for 14-carbon hydroxy fatty acids, as it can transfer other fatty acids, including odd-chain fatty acids, if they are available to the organism [5].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxyarachidonoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2-N-((3R)-3-hydroxyarachidonoyl)-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
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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
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additional information
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxyarachidonoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
UDP-2-N-((3R)-3-hydroxyarachidonoyl)-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
show the reaction diagram
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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buetow, L.; Smith, T.K.; Dawson, A.; Fyffe, S.; Hunter, W.N.
Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis
Proc. Natl. Acad. Sci. USA
104
4321-4326
2007
Chlamydia trachomatis (P0CD76), Chlamydia trachomatis
Manually annotated by BRENDA team