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Literature summary for 3.2.1.51 extracted from

  • Focarelli, R.; Cacace, M.G.; Seraglia, R.; Rosati, F.
    A nonglycosylated, 68-kDa alpha-L-fucosidase is bound to the mollusc bivalve Unio elongatulus sperm plasma membrane and differs from a glycosylated 56-kDa form present in the seminal fluid (1997), Biochem. Biophys. Res. Commun., 234, 54-58.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.71
-
4-nitrophenyl-alpha-L-fucopyranoside sperm-bound enzyme Unio elongatulus
0.91
-
4-nitrophenyl-alpha-L-fucopyranoside gonad fluid enzyme Unio elongatulus

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane
-
Unio elongatulus 5886
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55970
-
gonad fluid enzyme, mass spectrometry Unio elongatulus
55971
-
1 * 55971, gonad fluid enzyme, 1 * 67847, sperm-bound enzyme, mass spectrometry Unio elongatulus
67847
-
1 * 55971, gonad fluid enzyme, 1 * 67847, sperm-bound enzyme, mass spectrometry Unio elongatulus
67850
-
sperm-bound enzyme, mass spectrometry Unio elongatulus

Organism

Organism UniProt Comment Textmining
Unio elongatulus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein N-linked oligosaccharides only for the gonad fluid enzyme, sperm-bound enzyme not N- or O-linked glycosylated Unio elongatulus

Purification (Commentary)

Purification (Comment) Organism
to homogeneity, two forms, affinity chromatography Unio elongatulus

Source Tissue

Source Tissue Comment Organism Textmining
gonad fluid Unio elongatulus
-
semen one form tightly bound to the sperm plasma membrane, one form present in the gonad fluid Unio elongatulus
-

Storage Stability

Storage Stability Organism
4°C, 10 mM sodium phosphate, pH 5.5, 1 mM EDTA, 1 mM PMSF, one month Unio elongatulus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl-alpha-L-fucopyranoside + H2O
-
Unio elongatulus 4-nitrophenol + alpha-L-fucose
-
?

Subunits

Subunits Comment Organism
monomer 1 * 55971, gonad fluid enzyme, 1 * 67847, sperm-bound enzyme, mass spectrometry Unio elongatulus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50 60
-
Unio elongatulus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
gonad fluid enzyme sharper pH dependence curve than the sperm-bound enzyme Unio elongatulus