Literature summary for 3.2.1.70 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 .

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
F262A	the mutant enzyme has a stronger preference for transglucosylation than that of the wild type enzyme	Streptococcus mutans serotype c
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	?	-	?
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

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

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
4-nitrophenyl alpha-D-glucopyranoside + H2O	-	Streptococcus mutans serotype c	4-nitrophenol + D-glucopyranose	-	?
4-nitrophenyl alpha-D-glucopyranoside + H2O	-	Streptococcus mutans serotype c ATCC 700610	4-nitrophenol + D-glucopyranose	-	?
isomaltose + H2O	-	Streptococcus mutans serotype c	2 D-glucose	-	?
isomaltose + H2O	-	Streptococcus mutans serotype c ATCC 700610	2 D-glucose	-	?
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	?	-	?
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

Synonyms	Comment	Organism
dextran glucosidase	-	Streptococcus mutans serotype c