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Literature summary extracted from

  • Kobayashi, M.; Saburi, W.; Nakatsuka, D.; Hondoh, H.; Kato, K.; Okuyama, M.; Mori, H.; Kimura, A.; Yao, M.
    Structural insights into the catalytic reaction that is involved in the reorientation of Trp238 at the substrate-binding site in GH13 dextran glucosidase (2015), FEBS Lett., 589, 484-489 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.70 expressed in Escherichia coli BL21 (DE3) CodonPlus-RIL cells Streptococcus mutans serotype c

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.70 sitting drop vapor diffusion method. Mutant E236Q glucosyl-enzyme intermediate are obtained by co-crystallization with 5 mM alpha-D-glucosyl fluoride at 100 mM Tris-HCl (pH 7.5), 200 mM calcium chloride and 18% (w/v) polyethylene glycol (PEG) 6000. The ligand-free E236Q crystals are grown by using 100 mM sodium 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (pH 7.4), 200 mM calcium chloride and 18% (w/v) PEG 6000 Streptococcus mutans serotype c

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.70 F262A the mutant enzyme has a stronger preference for transglucosylation than that of the wild type enzyme Streptococcus mutans serotype c
3.2.1.70 F262W the mutant enzyme has a weaker preference for transglucosylation than that of the wild type enzyme Streptococcus mutans serotype c

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.70 additional information Streptococcus mutans serotype c the enzyme catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form alpha-(1->6)-glucosidic linkage at the substrate non-reducing ends ?
-
 ?
3.2.1.70 additional information Streptococcus mutans serotype c ATCC 700610 the enzyme catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form alpha-(1->6)-glucosidic linkage at the substrate non-reducing ends ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.70 Streptococcus mutans serotype c Q99040
-
-
3.2.1.70 Streptococcus mutans serotype c ATCC 700610 Q99040
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.70 Ni-chelating column chromatography and Superdex 200 gel filtration Streptococcus mutans serotype c

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.70 4-nitrophenyl alpha-D-glucopyranoside + H2O
-
 Streptococcus mutans serotype c 4-nitrophenol + D-glucopyranose
-
 ?
3.2.1.70 4-nitrophenyl alpha-D-glucopyranoside + H2O
-
 Streptococcus mutans serotype c ATCC 700610 4-nitrophenol + D-glucopyranose
-
 ?
3.2.1.70 isomaltose + H2O
-
 Streptococcus mutans serotype c 2 D-glucose
-
 ?
3.2.1.70 isomaltose + H2O
-
 Streptococcus mutans serotype c ATCC 700610 2 D-glucose
-
 ?
3.2.1.70 additional information the enzyme catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form alpha-(1->6)-glucosidic linkage at the substrate non-reducing ends Streptococcus mutans serotype c ?
-
 ?
3.2.1.70 additional information the enzyme catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form alpha-(1->6)-glucosidic linkage at the substrate non-reducing ends Streptococcus mutans serotype c ATCC 700610 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.70 dextran glucosidase
-
 Streptococcus mutans serotype c