2.7.7.23: UDP-N-acetylglucosamine diphosphorylase
This is an abbreviated version!
For detailed information about UDP-N-acetylglucosamine diphosphorylase, go to the full flat file.
Word Map on EC 2.7.7.23
Reaction
Synonyms
acetylglucosamine 1-phosphate uridylyltransferase, AGX-1, AGX1, AGX2, amino-sugar-1-phosphate acetyltransferase, bifunctional N-acetyltransferase/uridylyltransferase, BmUAP, CL6EHI_021200, CL6EHI_039830, EcGlmU, EnhiA.01126.a, EnhiA.01126.b, GlcNAc-1-P uridyltransferase, GlcNAc-1-P UTase, GlcNAc-1-phosphate nucleotidylyltransferase, GLCNAC1PUT1, GLCNAC1PUT2, GlmU, GlmUMTB, hiGlmU, LmUAP1, LmUAP2, LOC_Os08g10600, Mmy, More, mummy, N-acetyl-D-glucosamine-1-phosphate uridylyltransferase, N-acetyl-glucosamine-1-phosphate uridyltransferase, N-acetylglucosamine 1-phosphate uridyltransferase, N-acetylglucosamine-1-phosphate uridyltransferase, N-acetylglucosamine-1-phosphate uridylyltransferase, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase, Os08g10600, Rv1018c, spl29, spotted leaf 29, ST0452, ST0452 protein, STK_04520, Tb11.02.0120, UAP, UAP enzyme, UAP1, UAP2, UDP N-acetylglucosamine pyrophosphorylases 1, UDP N-acetylglucosamine pyrophosphorylases 2, UDP-GlcNAc pyrophosphorylase, UDP-GlcNAc pyrophosphorylase (UAP), UDP-HexNAc pyrophosphorylase, UDP-N-acetylgalactosamine pyrophosphorylase, UDP-N-acetylglucosamine diphosphorylase 1, UDP-N-acetylglucosamine diphosphorylase 2, UDP-N-acetylglucosamine pyrophosphorylase, UDP-N-acetylglucosamine pyrophosphorylase (UAP), UDP-N-acetylglucosamine pyrophosphorylase 1, UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase, UDP-N-acetylglucosamine-diphosphorylase, UDP-N-acetylhexosamine pyrophosphorylase, UDPacetylglucosamine pyrophosphorylase, UNAcP, uridine diphosphate N-acetylglucosamine pyrophosphorylase, uridine diphosphate-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine phosphorylase, uridine diphosphoacetylglucosamine pyrophosphorylase, uridine-diphospho-N-acetylglucosamine pyrophosphorylase, UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate uridylyltransferase, UTP:N-acetylglucosamine-1-P uridylyltransferase, Ydl103c protein
ECTree
2.7.7.23 UDP-N-acetylglucosamine diphosphorylaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
generation of a three-dimensional model, using human GlcNAc1p nucleotidyltransferase complexed with UDP-GlcNAc, PDB code 1JV1
purified recombinant His-tagged enzyme, sitting-drop vapor-diffusion method, mixing of 400 nl of 96.3 mg/ml protein in 25 mM HEPES, pH 7.0, 500 mM NaCl, 5% v/v glycerol, 2 mM DTT, 0.025% w/v azide, with 400 nl of crystallization solution containing 0.2 M lithium sulfate, 0.1 M Bis-Tris, pH 5.5, 25% w/v PEG 3350, 16°C, 1 week, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using residues 68-407 of human UAP isoform 1, PDB ID 1jv1, as a search model
to 1.8 A resolution. UAP exhibits the same three-domain global architecture as other UAPs, it appears to lack three alpha-helices at the N-terminus and contains two amino acids in the allosteric pocket that make it appear more like the human enzyme than that from Trypanosoma brucei
a 1.9 A resolution crystal structure of a synthetic small-molecule inhibitor (4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide) of GlmU is presented. The determined crystal structure indicate that the inhibitor occupies an allosteric site adjacent to the GlcNAc-1-P substrate-binding region, thus, preventing structural rearrangements that are required for the enzymatic reaction
purified recombinant detagged AGX1A229T in complex with UDP-GlcNAc, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement using the published AGX1 structure (PDB ID 1JV1) as a search model
structure-based drug design studies. The molecular recognition of the enzyme with the substrates occurs mainly by hydrogen bonds between ligands and Arg116, Arg383, Gly381, and Lys408 amino acids, and few hydrophobic interactions with Tyr382 and Lys123 residues
apo GlmU is crystallized at 20 °C using the sitting-drop vapor diffusion methodcrystal structure of a mimic of the Michaelis complex, with glucose 1-phosphate and acetyl-coenzyme A, helps us to propose the residues involved in deprotonation of glucosamine 1-phosphate and the loop movement that likely generates the active site required for glucosamine 1-phosphate to bind
GlmUMtb active site crystal structure analysis, PDB ID 3DJ4, and crystal structure of GlmU with both substrates (i.e., GlcNAc-1-P and UTP) in the presence of metal ions, soaking of GlmUMtb[Apo] crystals in a solution containing GlcNAc-1-P, UTP and MgCl2. the soaking solution consists of 10% PEG 8000, 100 mM HEPES, pH 7.5, 20 mM MgCl2, and 4 mM CoCl2, and substrate 50 mM GlcNAc-1-phosphate, with or without 10 mM UTP, for 4 h at 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution using molecular replacement with GlmUMtb[Apo] as a search model
GlmUMtb in complex with substrates/products bound at the acetyltransferase active site, sitting drop vapor diffusion method, mixing of 400 nl of 15 mg/ml protein, 5 mM acetyl-CoA, 5 mM MgCl2, 5 mM UDP-GlcNAc with 400 nl of 18% PEG 3350, 0.1 M Tris-Cl, pH 8.5, and 2% tacsimate, 4-8 days, for enzyme complex with CoA and N-acetylglucosamine-1-phosphate, acetyl-Coa-containing crystals are soaked in 5 mM GlcN-1-P, 5 mM MgCl2, 5 mM UDP-GlcNAc, 5 mM acetyl-CoA, 18% PEG 3350, 0.1 M Tris-Cl, pH 8.5, and 2% tacsimate, or by co-crystallizing the enzyme with 5 mM GlcNAc-1-P, 5 mM MgCl2, 5 mM UDPGlcNAc, and 5 mM CoA under the conditions mentioned for obtaining GlmUMtb(AcCoA) crystals, X-ray diffraction structure determination and analysis at 1.98-2.33 A resolution
hanging drop vapour diffusion method, using 20% PEG 3350, 0.15 M DL-malate pH 7.0
-
purified enzyme complexed with ATP and N-acetyl-alpha-D-glucosamine 1-phosphate, soaking apo GlmUMtb crystals in soaking solution consisting of 10% PEG 8000, 100 mM HEPES, pH 7.5, 20 mM MgCl2, 4 mM CoCl2, 10 mM ATP, and 10 mM GlcNAc-1-P at 4°C, the ligand-bound crystals are cryoprotected in a cryosolution consisting of 20% ethylene glycol, 15% PEG 8000, 100 mM HEPES, pH 7.5, 20 mM MgCl2, and 4 mM CoCl2, X-ray diffraction structure determination and analysis at 1.98 A resolution
-
purified recombinant enzyme mutant Y97N in complex with UTP or N-acetyl-alpha-D-glucosamine 1-phosphate, sitting drop vapor diffusion method, mixing of 11 mg/ml protein with ligands 5 mM UDP-GlcNAc and 10 mM (NH4)2SO4 (to form the complex with UDP-GlcNAc) or 5 mM UTP and 10 mM (NH4)2SO4 (to form the complex with UTP), and with crystallization solution containing 20% w/v PEG 3350 and 0.2 M potassium citrate tribasic monohydrate, X-ray diffraction structure determination and analysis at 2.91 and 2.09 A resolution, respectively
sitting drop vapor diffusion method at 22°C, crystallization of the Y97N protein
purified recombinant detagged enzyme in complex with inhibitor 1, sitting-drop vapor diffusion method, mixing of 500 nl of 15 mg/ml protein solution wit 500 nl of precipitant solution containing 25% PEG 3350, 0.2 M (NH4)2SO4, 0.1 M Bis-Tris, pH 5.5, 22°C, X-ray diffraction structure determination and analysis at 1.75 A resolution
-
in complex with inhibitor 3-[2-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one. Only the (R)-enantiomer binds, and it is likely that the kinked shape of the molecule is crucial for its shape-complimentarity to the pocket. The benzo[1,3]dioxole moiety is deeply buried, making close contact with Ala397 and Gly232 at the bottom of the cleft. The indolin-2-one sits at the top of the cleft, with the unsubstituted edge exposed to solvent and the methyl and bromide substituents on making contact with Ala239, Met370, Lys371, and Ala367
homology modeling of structure based on Haemophilus influenzae enzyme, PDB entry 2V0K
