Differences in the Substrate Specificities and Active-Site Structures of Two α-L-Fucosidases (Glycoside Hydrolase Family 29) fromBacteroides thetaiotaomicron | Zendy

Haruko Sakurama | Zendy; Erika Tsutsumi | Zendy; Hisashi Ashida | Zendy; Takane Katayama | Zendy; Kenji Yamamoto | Zendy; Hidehiko Kumagai | Zendy

Open Access

Differences in the Substrate Specificities and Active-Site Structures of Two α-L-Fucosidases (Glycoside Hydrolase Family 29) fromBacteroides thetaiotaomicron

Author(s) -

Haruko Sakurama,

Erika Tsutsumi,

Hisashi Ashida,

Takane Katayama,

Kenji Yamamoto,

Hidehiko Kumagai

Publication year - 2012

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.111004

Subject(s) - bacteroides thetaiotaomicron , glycoside hydrolase , active site , hydrolase , substrate (aquarium) , enzyme , stereochemistry , phylogenetic tree , substrate specificity , biochemistry , bacteroides , biology , chemistry , genetics , bacteria , ecology , gene

Recent studies suggest that α-L-fucosidases of glycoside hydrolase family 29 can be divided into two subfamilies based on substrate specificity and phylogenetic clustering. To explore the validity of this classification, we enzymatically characterized two structure-solved α-L-fucosidases representing the respective subfamilies. Differences in substrate specificities are discussed in relation to differences in active-site structures between the two enzymes.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research