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Bifunctional properties and characterization of a novel sialidase with esterase activity from Bifidobacterium bifidum
- Source :
- Bioscience, biotechnology, and biochemistry. 82(11)
- Publication Year :
- 2018
-
Abstract
- Sialidases catalyze the removal of terminal sialic acid from various complex carbohydrates. In the gastrointestinal tract, sialic acid is commonly found in the sugar chain of mucin, and many enteric commensals use mucin as a nutrient source. We previously identified two different sialidase genes in Bifidobacterium bifidum, and one was cloned and expressed as an extracellular protein designated as exo-α-sialidase SiaBb2. The other exo-α-sialidase gene (siabb1) from the same bifidobacterium encodes an extracellular protein (SiaBb1) consisting of 1795 amino acids with a molecular mass of 189 kDa. SiaBb1 possesses a catalytic domain that classifies this enzyme as a glycoside hydrolase family 33 member. SiaBb1 preferentially hydrolyzes α2,3-linked sialic acid over α2,6-linked sialic acid from sialoglycan, which is the same as SiaBb2. However, SiaBb1 has an SGNH hydrolase domain with sialate-O-acetylesterase activity and an N-terminal signal sequence and C-terminal transmembrane region. SiaBb1 is the first bifunctional sialidase identified with esterase activity. Abbreviations: GalNAc: N-acetyl-D-galactosamine; Fuc: L-fucose; Gal: D-galactose
- Subjects :
- 0301 basic medicine
ved/biology.organism_classification_rank.species
Sialate O-acetylesterase
Neuraminidase
Sialidase
Applied Microbiology and Biotechnology
Biochemistry
Esterase
Analytical Chemistry
Substrate Specificity
03 medical and health sciences
chemistry.chemical_compound
Catalytic Domain
Hydrolase
Glycoside hydrolase
Amino Acid Sequence
Cloning, Molecular
Molecular Biology
chemistry.chemical_classification
Bifidobacterium bifidum
Sequence Homology, Amino Acid
ved/biology
Hydrolysis
Organic Chemistry
Mucins
General Medicine
Sialic acid
Amino acid
030104 developmental biology
chemistry
Acetylesterase
Biotechnology
Subjects
Details
- ISSN :
- 13476947
- Volume :
- 82
- Issue :
- 11
- Database :
- OpenAIRE
- Journal :
- Bioscience, biotechnology, and biochemistry
- Accession number :
- edsair.doi.dedup.....7522c7f805b7bbe59ad42fb74f5c68dc