2.4.1.143: alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

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For detailed information about alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, go to the full flat file.

Reaction

Synonyms

2-beta-N-acetylglucosaminyltransferase, acetylglucosaminyltransferase II, alpha-1,6-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase, alpha-1,6-mannosylglycoprotein beta-1-2-N-acetylglucosaminyltransferase, beta-1,2-N-acetylglucosaminyltransferase II, BmGnTII, EC 2.4.1.51, GlcNAc-T II, GlcNAcT-II, GlcNAcTase-II, GnT II, Gnt II-A, Gnt II-B, GnT-II, GnTII, Mgat2, N-acetylglucosaminyltransferase II, N-acetylglucosaminyltransferase-II, N-acetylglucosaminyltransferases II, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II, TbGnTII, TbGT15, TTV/DEXT1, UDP-GlcNAc:alpha6-D-mannoside beta1,2-N-acetylglucosaminyltransferase II, UDP-GlcNAc:mannoside alpha1-6 acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-alpha-1,6-mannosylglycoprotein beta-1-2-N-acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-alpha-D-mannoside beta1-2-acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-mannoside alpha1->6-acetylglucosaminyltransferase

ECTree

     2 Transferases

         2.4 Glycosyltransferases

             2.4.1 Hexosyltransferases

                2.4.1.143 alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

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Results	in table
4	Activating Compound
2043	AA Sequence
1	Application
4	CAS Registry Number
14	Cloned(Commentary)
1	Crystallization (Commentary)
34	Disease/ Diagnostics
1	Expression
20	General Information
3	General Stability
17	Inhibitors
16	kcat/KM [mM/s]
5	Ki Value [mM]
35	KM Value [mM]
21	Localization
14	Metals/Ions
8	Molecular Weight [Da]
12	Natural Substrates/ Products (Substrates)
49	Organism
5	Pathway
6	PDB ID
10	pH Optimum
1	pH Range
3	Posttranslational Modification
13	Protein Variants
9	Purification (Commentary)
1	Reaction
1	Reaction Type
47	Reference
57	Source Tissue
6	Specific Activity [micromol/min/mg]
3	Storage Stability
66	Substrates and Products (Substrate)
7	Subunits
54	Synonyms
1	Systematic Name
12	Temperature Optimum [°C]
1	Temperature Stability [°C]
16	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.4.1.143 - alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified recombinant catalytic domain of MGAT2 at 20 mg/ml in 5 mM MnCl2, 10 mM HEPES, pH 7.0, 50 mM NaCl, 200 mM betaine, and 10% glycerol is crystallized using hanging drop vapor diffusion method from a reservoir of 1.4 M ammonium sulfate. Crystals grow in 8-12 weeks and are derivatized with uranium oxide for phasing. The crystals are transferred to the reservoir solution supplemented with 20% cryoprotectant (2:2:1 ratio of ethylene glycol:DMSO:glycerol). MGAT2:UO2 crystallizes in space group P43212. For the UDP complex (MGAT2:UDP), 20 mg/ml of protein containing 5 mM UDP, 5 mM MnCl2, 10 mM HEPES, pH 7.0, 50 mM NaCl, 200 mM betaine and 10% glycerol produces multinucleated crystals from a reservoir containing 1.9 M ammonium sulfate, 100 mM HEPES at pH 7.5. Crystal seeding and optimization produce single crystals from a reservoir containing 1.7 M ammonium sulfate, 100 mM HEPES, pH 7.5, 5 mM UDP, and 5 mM MnCl2. Crystals are transferred to a reservoir solution supplemented with 20% cryoprotectant (2:2:1 ratio of ethylene glycol, DMSO, and glycerol). MGAT2:UDP crystallizes in P21. For the acceptor complex (MGAT2:Acc), 20 mg/ml of protein in 5 mM acceptor (GlcNAc-Man3-GlcNAc2-Asn), 10 mM HEPES, pH 7.0, 50 mM NaCl, 200 mM betaine and 10% glycerol, is crystallized from 1.6 M ammonium sulfate, 100 mM HEPES, pH 7.5, using the MGAT2:UDP crystals as the initial seed stock and MGAT2:Acc crystals as the final seed stock. The crystals are cryoprotected with the reservoir solution supplemented with 5 mM acceptor, 1.6 M ammonium sulfate, 100 mM HEPES, pH 7.5, and 20% cryoprotectant (2:2:1 ratio of ethylene glycol, DMSO and glycerol). MGAT2:Acc crystallizes in P22121. X-ray diffraction structure determination and analysis at 2.0 A, 1.6 A, and 2.8 A resolution, respectively

Homo sapiens

Q10469

760070