2.3.1.191: UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase

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For detailed information about UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase, go to the full flat file.

Reaction

Synonyms

acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase, acyltransferase LpxD, CtLpxD, EcLpxD, firA, La0512, LpxD, LpxD1, Lpxd2, PA3646, UDP-3-O-(R-3-hydroxyacyl)-glucosamine acyltransferase, UDP-3-O-acyl-glucosamine N-acyltransferase

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.191 UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase

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Results	in table
1	Activating Compound
23563	AA Sequence
1	Application
14	Cloned(Commentary)
6	Crystallization (Commentary)
22	General Information
2	IC50 Value
11	Inhibitors
11	kcat/KM [mM/s]
7	Ki Value [mM]
25	KM Value [mM]
2	Localization
3	Molecular Weight [Da]
9	Natural Substrates/ Products (Substrates)
33	Organism
11	Pathway
45	PDB ID
2	pH Optimum
16	Protein Variants
7	Purification (Commentary)
1	Reaction
29	Reference
2	Source Tissue
2	Specific Activity [micromol/min/mg]
21	Substrates and Products (Substrate)
4	Subunits
32	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
24	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.3.1.191 - UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

apo forms of LpxD in space groups P21 and P4322, to 2.7 and 2.8 A resolution, respectively. The asymmetric unit contains two protein trimers

Acinetobacter baumannii

B0VMV2

735384

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

P0CD76

700935

enzyme in complex with 4-(2-chlorophenyl)-3-hydroxy-7,7-dimethyl-2-phenyl-7,8-dihydro-2H-pyrazolo[3,4-b]quinolin-5(6H)-one. Enzyme in complex with 3-hydroxy-7,7-dimethyl-2-phenyl-4-(thiophen-2-yl)-7,8-dihydro-2H-pyrazolo[3,4-b]-quinolin-5(6H)-one

Escherichia coli

Q0P6M7

755699

hanging drop/vapor diffusion method. The crystal structure of N-terminally His6-tagged EcLpxD is determined by molecular replacement at 2.6 A resolution, using Chlamydia trachomatis (PDB code: 2IUA) as the model. Comparison of LpxD from Escherichia coli and Chlamydia trachomatis. Attempts to crystallize EcLpxD with UDP-GlcNAc, UDP-3-O-(R-3-hydroxymyristoyl)-R-D-GlcNAc or its product UDP-2,3-diacylglucosamine are unsuccessful

Escherichia coli

P21645

696356

in complex with three forms of acyl carrier protein. Interactions at the interface optimally position acyl carrier protein for acyl delivery and directly involve the pantetheinyl group

Escherichia coli

P21645

736880

purified recombinant His6-tagged LpxD, hanging drop vapour diffusion, 0.002 ml of 15 mg/ml LpxD in 10 mM Tris pH 8, 500 mM NaCl and 1 mM DTT, with 50 mM uridine diphosphate-N-acetylglucosamine, is mixed with 0.002 ml of 100 mM Tris pH 8.5, 1.5 M lithium sulfate, 20°C, 3-5 days, X-ray diffraction structure determination and analysis at 1.3 A resolution, molecular replacement

Pseudomonas aeruginosa

Q9HXY6

718513