β-D-Fucosidase

(Redirected from EC 3.2.1.38)

β-D-Fucosidase (EC 3.2.1.38, β-fucosidase) is an enzyme with systematic name β-D-fucoside fucohydrolase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

β-D-Fucosidase
Identifiers
EC no.3.2.1.38
CAS no.9025-34-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins
Hydrolysis of terminal non-reducing β-D-fucose residues in β-D-fucosides

Enzymes from some sources also hydrolyse β-D-galactosides, β-D-glucosides and α-L-arabinosides.

References

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  1. ^ Chinchetru MA, Cabezas JA, Calvo P (1983). "Characterization and kinetics of β-D-gluco/fuco/galactosidase from sheep liver". Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 75 (4): 719–28. doi:10.1016/0305-0491(83)90124-4. PMID 6413126.
  2. ^ Chinchetru MA, Cabezas JA, Calvo P (1989). "Purification and characterization of a broad specificity β-glucosidase from sheep liver". The International Journal of Biochemistry. 21 (5): 469–76. doi:10.1016/0020-711X(89)90126-2. PMID 2503402.
  3. ^ Rodriguez JA, Cabezas JA, Calvo P (1982). "β-Fucosidase, β-glucosidase and β-galactosidase activities associated in bovine liver". The International Journal of Biochemistry. 14 (8): 695–8. doi:10.1016/0020-711X(82)90003-9. PMID 6811346.
  4. ^ Wiederschain GY, Prokopenkov AA (October 1973). "β-D-Galactosidase and β-D-fucosidase of pig kidney". Archives of Biochemistry and Biophysics. 158 (2): 539–43. doi:10.1016/0003-9861(73)90546-8. PMID 4782520.
  5. ^ Beyer EM, Klyashchitsky BA, Shashkov AS (June 1981). "Specificity patterns of different types of human fucosidase. Recognition of a certain region of the pyranose ring in sugars by the enzymes". Biochimica et Biophysica Acta. 659 (2): 434–44. doi:10.1016/0005-2744(81)90069-3. PMID 6789883.
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