2.7.7.13: mannose-1-phosphate guanylyltransferase

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For detailed information about mannose-1-phosphate guanylyltransferase, go to the full flat file.

Reaction

Synonyms

BceA, BceA(J) protein, BceAJ, CYT1, GDP-alpha-D-mannose pyrophosphorylase, GDP-D-mannose pyrophosphorylase, GDP-Man pyrophosphorylase, GDP-mannose pyrophosphorylase, GDP-mannose pyrophosphorylase B, GDP-ManPP, GDP-MP, GDPMan pyrophosphorylase, GMP, GMP3, GMPase, GMPBB, GMPP, GMPP1, GMPP2, GMPP3, GMPPB, GTP-alpha-D-Man-1-P guanylyltransferase, GTP-mannose 1-phosphate guanylyltransferase, GTP-mannose-1-phosphate guanylyltransferase, guanidine diphosphomannose pyrophosphorylase, guanidine diphosphomannose pyrophoyphorylase, guanosine 5'-diphosphate-mannose pyrophosphorylase, guanosine 5'-diphospho-D-mannose pyrophosphorylase, guanosine diphosphate mannose pyrophosphorylase, guanosine diphosphate mannose pyrophosphorylase B, guanosine diphosphate-mannose pyrophosphorylase, guanosine diphosphomannose pyrophosphorylase, guanosine triphosphate-mannose 1-phosphate guanylyltransferase, guanosine-diphospho-D-mannose pyrophosphorylase, guanylyltransferase, mannose 1-phosphate, LDBPK_230120, Man-1-PGTase, mannose 1-phosphate guanyltransferase, mannose 1-phosphate guanylyltransferase (guanosine triphosphate), mannose-1-phosphate guanyl transferase, mannose-1-phosphate guanyltransferase beta, mannose-1-phosphate guanylyltransferase, More, MPG, MPG transferase, multiple sugar-1-P NTase, NDP-sugar pyrophosphorylase, NSPase, Os01g0847200, Os03g0268400, OsVTC1-1, OsVTC1-3, OsVTC1-8, PFManC, PH0925, PH0925 protein, PIM-GMP, RfbM, VCT1-1, VCT1-3, VTC1, VTC1-1, VTC1-3

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.7 Nucleotidyltransferases

                2.7.7.13 mannose-1-phosphate guanylyltransferase

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Results	in table
1	Activating Compound
22195	AA Sequence
8	Application
1	CAS Registry Number
39	Cloned(Commentary)
4	Crystallization (Commentary)
131	Disease/ Diagnostics
12	Expression
47	General Information
10	IC50 Value
60	Inhibitors
1	kcat/KM [mM/s]
12	Ki Value [mM]
71	KM Value [mM]
13	Localization
57	Metals/Ions
31	Molecular Weight [Da]
57	Natural Substrates/ Products (Substrates)
152	Organism
8	Pathway
39	PDB ID
21	pH Optimum
1	pH Range
1	pH Stability
5	pI Value
29	Protein Variants
26	Purification (Commentary)
4	Reaction
1	Reaction Type
77	Reference
1	Renatured (Commentary)
38	Source Tissue
13	Specific Activity [micromol/min/mg]
7	Storage Stability
152	Substrates and Products (Substrate)
36	Subunits
159	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]
6	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.7.13 - mannose-1-phosphate guanylyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

ligand-free enzyme, sitting drop vapor diffusion method, using 0.1 M bis-Tris pH 6.5, 25% (w/v) PEG 3350, 0.2 M lithium sulfate. Enzyme bound to GTP and D-mannose 1-phosphate, sitting drop vapor diffusion method, using 0.1 M magnesium formate, 15% (w/v) PEG 3350

Arabidopsis thaliana

O22287

760288

comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. The human active site is site very similar to the Leishmania donovani one. Leishmania donovani GDP-mannose diphosphorylase makes more interactions with its substrate than the human enzyme does

Homo sapiens

Q9Y5P6

738156

comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. Residues Leu14, Val15, Ala60, Leu92 and Pro97 surround the hydrophobic bicycle of the nucleotide, while the amine groups of the latter interact with Glu88. The ribose ring belonging to the substrate is bound to protein residues Asn116 and Ser117. The magnesium ion is chelated by Asp118 and Asp226, and the diphosphate group makes electrostatic interactions with residues Arg21 and Lys31, which belong to the GGXGXRLXPLX5PK diphosphorylase signature

Leishmania donovani

E9BG32

738156

enzyme in apo form, in complex with substrates mannose-1-phosphate, or with GTP, or bound to the end product GDP-Mannose and Mg2+, sitting drop vapour diffusion method, for apoenzyme: mixing of equal volumes of 20 mg/ml protein in 10 mM Tris, pH 8.0, 150 mM NaCl with reservoir solution containing 35% v/v 2-methyl-2,4-pentanediol, 0.1 M phosphate citrate, pH 7.5, for enzyme complexes: preincubation of 12.5 or 25 mg/ml protein in 10 mM HEPES, pH 7.5, 100 mM NaCl, 10 mM MgCl2, with a 16:1 alpha-D-mannose 1-phosphate or a 8:1 GTP and GDP-Man molar excess of ligand for 30 min at room temperature, protein to well solution ratio of 3:1, the well solution containing 30-35% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, pH 4.6, 20 mM MgCl2, or in a 2:1 ratio with weel solution containing 30% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, pH 5.0, 20 mM MgCl2, X-ray diffraction structure determination and analysis at 2.1-2.95 A resolution

Thermotoga maritima

Q9X0C3

722682