Characterization of a new α-l-fucosidase isolated from Fusarium proliferatum LE1 that is regioselective to α-(1 → 4)-l-fucosidic linkage in the hydrolysis of α-l-fucobiosides. Shvetsova, S. V., Shabalin, K. A., Bobrov, K. S., Ivanen, D. R., Ustyuzhanina, N. E., Krylov, V. B., Nifantiev, N. E., Naryzhny, S. N., Zgoda, V. G., Eneyskaya, E. V., & Kulminskaya, A. A. Biochimie, 132:54–65, January, 2017.
doi  abstract   bibtex   
Here, we report the biochemical characterization of a novel α-l-fucosidase with broad substrate specificity (FpFucA) isolated from the mycelial fungus Fusarium proliferatum LE1. Highly purified α-l-fucosidase was obtained from several chromatographic steps after growth in the presence of l-fucose. The purified α-l-fucosidase appeared to be a monomeric protein of 67 ± 1 kDa that was able to hydrolyze the synthetic substrate p-nitrophenyl α-l-fucopyranoside (pNPFuc), with K (m) = 1.1 ± 0.1 mM and k (cat) = 39.8 ± 1.8 s (-1). l-fucose, 1-deoxyfuconojirimycin and tris(hydroxymethyl)aminomethane inhibited pNPFuc hydrolysis, with inhibition constants of 0.2 ± 0.05 mM, 7.1 ± 0.05 nM, and 12.2 ± 0.1 mM, respectively. We assumed that the enzyme belongs to subfamily A of the GH29 family (CAZy database) based on its ability to hydrolyze practically all fucose-containing oligosaccharides used in the study and the phylogenetic analysis. We found that this enzyme was a unique α-l-fucosidase that preferentially hydrolyzes the α-(1 → 4)-L-fucosidic linkage present in α-L-fucobiosides with different types of linkages. As a retaining glycosidase, FpFucA is capable of catalyzing the transglycosylation reaction with alcohols (methanol, ethanol, and 1-propanol) and pNP-containing monosaccharides as acceptors. These features make the enzyme an important tool that can be used in the various modifications of valuable fucose-containing compounds.
@Article{Shvetsova2017,
  author          = {Shvetsova, Svetlana V. and Shabalin, Konstantin A. and Bobrov, Kirill S. and Ivanen, Dina R. and Ustyuzhanina, Nadezhda E. and Krylov, Vadim B. and Nifantiev, Nikolay E. and Naryzhny, Stanislav N. and Zgoda, Victor G. and Eneyskaya, Elena V. and Kulminskaya, Anna A.},
  journal         = {Biochimie},
  title           = {Characterization of a new α-l-fucosidase isolated from Fusarium proliferatum LE1 that is regioselective to α-(1 → 4)-l-fucosidic linkage in the hydrolysis of α-l-fucobiosides.},
  year            = {2017},
  issn            = {1638-6183},
  month           = jan,
  pages           = {54--65},
  volume          = {132},
  abstract        = {Here, we report the biochemical characterization of a novel α-l-fucosidase with broad substrate specificity (FpFucA) isolated from the mycelial fungus Fusarium proliferatum LE1. Highly purified α-l-fucosidase was obtained from several chromatographic steps after growth in the presence of l-fucose. The purified α-l-fucosidase appeared to be a monomeric protein of 67 ± 1 kDa that was able to hydrolyze the synthetic substrate p-nitrophenyl α-l-fucopyranoside (pNPFuc), with K (m) = 1.1 ± 0.1 mM and k (cat) = 39.8 ± 1.8 s (-1). l-fucose, 1-deoxyfuconojirimycin and tris(hydroxymethyl)aminomethane inhibited pNPFuc hydrolysis, with inhibition constants of 0.2 ± 0.05 mM, 7.1 ± 0.05 nM, and 12.2 ± 0.1 mM, respectively. We assumed that the enzyme belongs to subfamily A of the GH29 family (CAZy database) based on its ability to hydrolyze practically all fucose-containing oligosaccharides used in the study and the phylogenetic analysis. We found that this enzyme was a unique α-l-fucosidase that preferentially hydrolyzes the α-(1 → 4)-L-fucosidic linkage present in α-L-fucobiosides with different types of linkages. As a retaining glycosidase, FpFucA is capable of catalyzing the transglycosylation reaction with alcohols (methanol, ethanol, and 1-propanol) and pNP-containing monosaccharides as acceptors. These features make the enzyme an important tool that can be used in the various modifications of valuable fucose-containing compounds.},
  chemicals       = {Alcohols, Disaccharides, Fungal Proteins, Glycosides, Oligosaccharides, Polysaccharides, fucopyranosyl-1-3-fucopyranose, Fucose, fucoidan, alpha-L-Fucosidase},
  citation-subset = {IM},
  completed       = {2017-01-30},
  country         = {France},
  doi             = {10.1016/j.biochi.2016.10.014},
  issn-linking    = {0300-9084},
  keywords        = {Alcohols, metabolism; Amino Acid Sequence; Disaccharides, metabolism; Fucose, metabolism; Fungal Proteins, genetics, isolation & purification, metabolism; Fusarium, enzymology, genetics; Glycosides, metabolism; Glycosylation; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Mass Spectrometry; Oligosaccharides, metabolism; Polysaccharides, metabolism; Stereoisomerism; Substrate Specificity; Temperature; alpha-L-Fucosidase, genetics, isolation & purification, metabolism; Fusarium proliferatum; Translycosylation; α-(1 → 4)-l-fucosidic linkage; α-l-fucobiosides; α-l-fucosidase},
  nlm-id          = {1264604},
  owner           = {NLM},
  pii             = {S0300-9084(16)30302-9},
  pmid            = {27984201},
  pubmodel        = {Print-Electronic},
  pubstate        = {ppublish},
  revised         = {2017-11-16},
}
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