Literature summary for 3.2.1.11 extracted from

Suzuki, N.; Kim, Y.M.; Fujimoto, Z.; Momma, M.; Okuyama, M.; Mori, H.; Funane, K.; Kimura, A.
Structural elucidation of dextran degradation mechanism by Streptococcus mutans dextranase belonging to glycoside hydrolase family 66 (2012), J. Biol. Chem., 287, 19916-19926.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Streptococcus mutans

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the conserved fragment from residue Gln100 to Ile732, devoid of its N- and C-terminal variable regions, 1.6 A resolution. Structural domain N possesses an immunoglobulin-like beta-sandwich fold, domain A contains the enzyme's catalytic module, comprising a (beta/alpha)8-barrel, and domain C forms a beta-sandwich structure containing two Greek key motifs. In the enzyme-isomaltotriose complex structure, the bound isomaltooligosaccharide with four glucose moieties is observed in the catalytic glycone cleft and considered to be the transglycosylation product of the enzyme, indicating the presence of four subsites in the catalytic cleft. The complexed structure with suicide substrate 4',5'-epoxypentyl-alpha-D-glucopyranoside reveals that the epoxide ring reacts to form a covalent bond with the Asp385 side chain. Asp385 is the catalytic nucleophile and Glu453 is the acid/base of the double displacement mechanism	Streptococcus mutans

Crystallization (Comment)

Organism

crystal structure of the conserved fragment from residue Gln100 to Ile732, devoid of its N- and C-terminal variable regions, 1.6 A resolution. Structural domain N possesses an immunoglobulin-like beta-sandwich fold, domain A contains the enzyme's catalytic module, comprising a (beta/alpha)8-barrel, and domain C forms a beta-sandwich structure containing two Greek key motifs. In the enzyme-isomaltotriose complex structure, the bound isomaltooligosaccharide with four glucose moieties is observed in the catalytic glycone cleft and considered to be the transglycosylation product of the enzyme, indicating the presence of four subsites in the catalytic cleft. The complexed structure with suicide substrate 4',5'-epoxypentyl-alpha-D-glucopyranoside reveals that the epoxide ring reacts to form a covalent bond with the Asp385 side chain. Asp385 is the catalytic nucleophile and Glu453 is the acid/base of the double displacement mechanism

Streptococcus mutans

Organism

Organism	UniProt	Comment	Textmining
Streptococcus mutans	Q54443	-	-
Streptococcus mutans ATCC 700610	Q54443	-	-

Synonyms

Synonyms	Comment	Organism
DexA	-	Streptococcus mutans

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)