2.5.1.7: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

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For detailed information about UDP-N-acetylglucosamine 1-carboxyvinyltransferase, go to the full flat file.

Reaction

Synonyms

enol-pyruvyltransferase, enolpyruvyl UDP-GlcNAc synthase, enoylpyruvate transferase, enoylpyruvatetransferase, EPT, More, MurA, MurA enzyme, MurA transferase, MurAA, MurZ, phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase, phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase, phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase, phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-deoxyglucose-3-enolpyruvyltransferase, phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase, pyruvate-UDP-acetylglucosamine transferase, pyruvate-uridine diphospho-N-acetyl-glucosamine transferase, pyruvate-uridine diphospho-N-acetylglucosamine transferase, pyruvatetransferase, phosphoenolpyruvate-uridine diphosphoacetylglucosamine, pyruvic-uridine diphospho-N-acetylglucosaminyltransferase, UDP-GlcNAc enolpyruvyl transferase, UDP-N-acetylglucosamine 1-carboxyvinyl transferase, UDP-N-acetylglucosamine 1-carboxyvinyl-transferase, UDP-N-acetylglucosamine 1-carboxyvinyltransferase, UDP-N-acetylglucosamine enolpyruvyl transferase, UDP-N-acetylglucosamine enolpyruvyle transferase, UDP-N-acetylglucosamine enolpyruvyltransferase, UDP-N-acetylglucosamine enoylpyruvyltransferase, UDP-N-acetylglucosamine-enolpyruvyl transferase, UDP-NAG enolpyruvyl transferase, UNAG enolpyruvyl transferase

ECTree

     2 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.7 UDP-N-acetylglucosamine 1-carboxyvinyltransferase

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Results	in table
4	Activating Compound
45128	AA Sequence
12	Application
1	CAS Registry Number
33	Cloned(Commentary)
12	Crystallization (Commentary)
29	General Information
3	General Stability
71	IC50 Value
374	Inhibitors
21	kcat/KM [mM/s]
38	Ki Value [mM]
50	KM Value [mM]
2	Localization
6	Metals/Ions
21	Molecular Weight [Da]
40	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
387	Organism
9	Pathway
166	PDB ID
13	pH Optimum
4	pH Range
1	pI Value
56	Protein Variants
31	Purification (Commentary)
37	Reaction
1	Reaction Type
104	Reference
10	Specific Activity [micromol/min/mg]
7	Storage Stability
115	Substrates and Products (Substrate)
24	Subunits
126	Synonyms
1	Systematic Name
12	Temperature Optimum [°C]
32	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.5.1.7 - UDP-N-acetylglucosamine 1-carboxyvinyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

in complex with UDP-N-acetylglucosamine and fosfomycin, sitting drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.1 M bis-Tris pH 6.5

Aliivibrio fischeri

B5F9P4

721232

at 19°C, from 10 mM MES, pH 6.4, 10% (w/v) polyethylene glycol 20000, in the presence of 5 mM UDP-N-acetyl-D-glucosamine and 5 mM phosphoenolpyruvate

Enterobacter cloacae

P33038

674498

crystallization of substrate-free enzyme, two-domain structure with an unusual fold, inside out alpha/beta barrel, which is built up from the 6fold repetititon of one folding unit, structure analysis

Enterobacter cloacae

-

637600

in complex with inhibitor T6361

Enterobacter cloacae

P33038

659457

in complex with substrates, hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 5.5), 0.2 M NH4OAc, 25% (w/v) PEG 3350

Enterobacter cloacae

P33038

722746

mutant D305A, in presence of phosphoenolpyruvate and UDP-N-acetyl-D-glucosamine

Enterobacter cloacae

-

659285

X-ray structure analysis of ligated and unligated MurA

Enterobacter cloacae

-

637601

crystallization of the enzyme complexed with UDP-N-acetylglucosamine and fosfomycin, two-domain structure with the active site located between them, structure and substrate binding analysis

Escherichia coli

-

637599

in complex with inhibitor cnicin and substrate UDP-N-acetylglucosamine, at 2.0 A resolution. The enzyme catalyzes the formation of a covalent adduct between cnicin and UDP-N-acetylglucosamine via an anti-Michael 1,3-addition of UDP-N-acetylglucosamine to an alpha,beta-unsaturated carbonyl function in cnicin thus forming a noncovalent suicide inhibitor

Escherichia coli

P0A749

688290

MurA is crystallized in the presence of sodium phosphite and UDP-N-acetylmuramic acid using the hanging drop vapor diffusion method, the MurA cocrystal structure with UDP-N-acetylmuramic acid and phosphite reveals a new staged MurA conformation in which the Arg397 side chain tracked phosphite out of the catalytic site

Escherichia coli

P0A749

702267

in complex with UDP-N-acetylglucosamine and fosfomycin, to 2.3 A resolution. The active-site loop can adopt one of the three major conformations: a fully open conformation, a half-open conformation, and a closed conformation. Fosfomycin can bind without inducing a large change in the half-open conformation of the binary complex with UDP-N-acetylglucosamine

Haemophilus influenzae

P45025

689975

in the apo-form, as well as in a complex with UDP-N-acetylglucosamine and fosfomycin using ammonium sulfate as the precipitant, hanging drop vapour diffusion method

Haemophilus influenzae

-

675932