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Literature summary extracted from

  • Miyazaki, T.; Ichikawa, M.; Iino, H.; Nishikawa, A.; Tonozuka, T.
    Crystal structure and substrate-binding mode of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8 (2015), J. Struct. Biol., 190, 21-30 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.170 gene Tt8MGH, recombinant expression in Escherichia coli strain BL21 (DE3) Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.106 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
3.2.1.170 purified enzyme free or in complexes with glucose or glycerate, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 10 mM Tris-HCl, pH 7.5, with 0.001 ml of reservoir solution containing 20-35% v/v 2-methyl-2,4-pentanediol and 100 mM Tris-HCl, pH 5.5-6.5, for co-crystallization with glucose or glycerate, the protein solution is mixed with 10 mM ligand solution, and stored at 4°C overnight. The Tt8MGH-Glc complex crystals are grown with the same method except that 100 mM sodium citrate buffer, pH 4.8-6.0, is used instead of Tris-HCl buffer in the reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.77-2.10 A resolution, molecular replacement method using PDB 2Z07 as a search model, modelling Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.106 48800
-
 calculated from sequence Thermus thermophilus
3.2.1.106 125400
-
 gel filtration Thermus thermophilus
3.2.1.170 125400
-
 recombinant enzyme, gel filtration Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.106 Thermus thermophilus Q5SJN0
-
-
3.2.1.170 Thermus thermophilus Q5SJN0
-
-
3.2.1.170 Thermus thermophilus ATCC 27634 Q5SJN0
-
-
3.2.1.170 Thermus thermophilus DSM 579 Q5SJN0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.106
-
 Thermus thermophilus
3.2.1.170 recombinant enzyme from Escherichia coli strain BL21 (DE3) by heat treatment at 70°C for 10 min, followed by hydrophobic interaction and anion exchange chromatography, to homogeneity Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.170 additional information conformational changes may be induced by ligand binding and serve to form finger-like structures for holding substrates, substrate recognition mechanism for GH63 mannosylglycerate hydrolase, overview Thermus thermophilus ?
-
 ?
3.2.1.170 additional information conformational changes may be induced by ligand binding and serve to form finger-like structures for holding substrates, substrate recognition mechanism for GH63 mannosylglycerate hydrolase, overview Thermus thermophilus DSM 579 ?
-
 ?
3.2.1.170 additional information conformational changes may be induced by ligand binding and serve to form finger-like structures for holding substrates, substrate recognition mechanism for GH63 mannosylglycerate hydrolase, overview Thermus thermophilus ATCC 27634 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.106 homotrimer 3 * 48800, calculated from sequence Thermus thermophilus
3.2.1.170 homotrimer 3 * 48800, about, sequence calculation Thermus thermophilus
3.2.1.170 More enzyme Tt8MGH consists of a single (alpha/alpha)6-barrel catalytic domain with two additional helices and two long loops which form a homotrimer, structure comparisons, overview. The conformations of three flexible loops are largely different from each other. The trimer is clover leaf-shaped Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.106 mannosylglycerate hydrolase
-
 Thermus thermophilus
3.2.1.106 Tt8MGH
-
 Thermus thermophilus
3.2.1.170 GH63 mannosylglycerate hydrolase
-
 Thermus thermophilus
3.2.1.170 Tt8MGH
-
 Thermus thermophilus

General Information

EC Number General Information Comment Organism
3.2.1.170 evolution the enzyme belongs to the glycosyl hydrolase family 63, GH 63 Thermus thermophilus