3.2.1.106: mannosyl-oligosaccharide glucosidase

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For detailed information about mannosyl-oligosaccharide glucosidase, go to the full flat file.

Reaction

Synonyms

(Glc3)-glucosidase, acid alpha-glucosidase, alpha-glucosidase I, CHO-GAA, CWH41, Cwh41p, GAA, GCSI, Glc I, Glc3 oligosaccharide glucosidase, Glc3-glucosidase, Glc3-oligosaccharide glucosidase, Glc3-OS-glucosidase, Glc3Man9GlcNAc2 oligosaccharide glucosidase, Glc3Man9NAc2 oligosaccharide glucosidase, glucosidase 1, glucosidase I, glucosidase, mannosyloligosaccharide, glucosidase-1, glycoengineered acid alpha-glucosidase, HP-GAA, K12 YgjK protein, KNOPF, mannosyl-oligosaccharide glucosidase, mannosylglycerate hydrolase, MOGS, oxime-neo-rhGAA, PGI, processing alpha-glucosidase I, processing exoglucosidase I, processing glucosidase I, rhGAA, tgGAA, trimming enzyme I, trimming glucosidase I, Tt8MGH, YgjK

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.106 mannosyl-oligosaccharide glucosidase

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Results	in table
19	Activating Compound
3273	AA Sequence
15	Application
1	CAS Registry Number
14	Cloned(Commentary)
2	Crystallization (Commentary)
1926	Disease/ Diagnostics
4	General Information
8	General Stability
11	IC50 Value
174	Inhibitors
15	Ki Value [mM]
9	KM Value [mM]
120	Localization
20	Metals/Ions
36	Molecular Weight [Da]
212	Natural Substrates/ Products (Substrates)
219	Organism
4	Pathway
5	PDB ID
21	pH Optimum
8	pH Range
2	pH Stability
3	pI Value
21	Posttranslational Modification
11	Protein Variants
25	Purification (Commentary)
8	Reaction
2	Reaction Type
67	Reference
47	Source Tissue
22	Specific Activity [micromol/min/mg]
14	Storage Stability
422	Substrates and Products (Substrate)
15	Subunits
79	Synonyms
1	Systematic Name
13	Temperature Optimum [°C]
6	Temperature Stability [°C]
2	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.106 - mannosyl-oligosaccharide glucosidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

1.8 A, hanging-drop vapour-diffusion method, 20°C, 30% PEG 8000, 0.6 M magnesium chloride, 100 mM Tris-HCl, pH 7.5, flash-frozen in a stream of nitrogen gas at -173°C

Escherichia coli

-

667038

1.67 A crystal structure and structures of the protein in complexes with glucose or glycerate are determined at 1.77 or 2.10 A resolution. Hanging-drop vapor diffusion method at 20°C

Thermus thermophilus

Q5SJN0

751418