Differences in the substrate specificities and active-site structures of two α-L-fucosidases (glycoside hydrolase family 29) from Bacteroides thetaiotaomicron.
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.
Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.
Haruko
H
Sakurama
Erika
E
Tsutsumi
Hisashi
H
Ashida
Takane
T
Katayama
Kenji
K
Yamamoto
Hidehiko
H
Kumagai
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001439:Bacteroides / Q000201:enzymology* / Q000235:genetics; D002240:Carbohydrate Sequence; D020134:Catalytic Domain; D004926:Escherichia coli; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D005644:alpha-L-Fucosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D007527:Isoenzymes; D011994:Recombinant Proteins; D005644:alpha-L-Fucosidase