P-D-Fucosidase

Luta, M., Hensel, A. and Kreis, W. (1997) p-D-Fucosidase and other cardenolide glycoside-modifying enzyme in Digitalis lanata EHRH, in 45th Annual Congress on Medicinal Plant Research, Regensburg. 

As a result of the structural similarity between o-fucose and D-galactose, most P-D-galactosidases are able to hydrolyze P-D-fucosides. Therefore, it is difficult to place P-D-fucosidases as a separate class of enzymes. The only exception to date is the P-D-fucosidase of A. phoenicis. This enzyme shows high specificity toward p-nitrophenyl-p-D-fucoside [32]. However, it does not hydrolyze / -nitrophenyl-P-D-Gal or jp-nitrophenyl-p-D-Glc. 

Fig. 6. The action of glycosidases on XXFG. a-L-Fucosidase (F) can attack at any time [37], whereas a-o-xylosidase (X) and P-D-glucosidase (G) must act in the sequence shown [35]. Other abbreviations...

H. Hashimoto, K. Shimada, and S. Horito, Synthesis of 1-6, 1-4 and 1-3 linked lthio-a-1-fucopyranosyl-2-acetamido-2-deoxy-P-D-glucopyranosides and 1-2 linked p-o-galactopyran-oside, and their linkage-specific inhibitory activities toward ot-L-fucosidases, Tetrahedron Lett., 34 (1993) 4953-4956. 

Human acid jS-D-galactosidase, jS-D-fucosidase, and a-L-arabinofuranosidase appear to have a common identity (see p. 429). 

The extents of sialylation of eleven plasma hydrolases have been examined. Most plasma hydrolases e.g. a-L-fucosidase and a-D-mannosidase) were eluted from DEAE-cellulose at a lower salt concentration after treatment with neuraminidase, although the elution profiles of p-D-glucosidase, P-D-xylosidase, and acid phosphatases were unaffected, indicating that they are less susceptible to the action of neuraminidase. The structure (9) assigned (G. Spick, B. Bayard, B. Fournet, and G. Strecker, F.E.B.S. Letters, 1975, 50, 296) to the carbohydrate component of human serotransferrin has been confirmed by high-resolution H n.m.r. spectroscopy. Electrophoresis separated human serotransferrin into four molecular forms that contain different proportions of bound iron. The nature of the interaction of renins from human and rabbit kidneys with immobilized concanavalin A, and their subsequent desorption with methyl a-D-mannopyrano-side, suggested that both proteins are glycosylated. ... 

Cobucci-Ponzano, B., Conte, F., Benelli, D., Londei, P., Flagiello, A., Monti, M., Pucci, P., Rossi, M. and Moracci, M. (2006). The gene of an archaeal alpha-L-fucosidase is expressed by translational frameshifting. Nucleic Acids Res, 34,4258-4268. 

Valk, P.J.M., Hoi, S., Vankin, Y, Ihle, J.N., Askew, D., Jenkins, N.A., Gilbert, D.J., Copeland, N.G., DE Both, N.J., Lowenberg, B., Delwel, R. (1997) The genes encoding the peripheral cannabinoid receptor and a-L-fucosidase are located near a newly identified common virus integration site, Evill. J. Virol. 71, 6796-6804. 

Decreased binding by the lectins concanavalin A and wheat-germ agglutinin has been found for a number of acidic hydrolases ( 3-D-2-acetamido-2-deoxy-hexosidase, a-L-fucosidase, a- and jS-D-glucosidase, jS-D-galactosidase, and a-D-mannosidase) from skin fibroblasts of three unrelated patients with mucolipidosis II (see p. 423). 

Investigation of the binding characteristics of urinary acid jS-D-galactosidase, j8-D-2-acetamido-2-deoxyglucosidase, a-D-galactosidase, and a-L-fucosidase from patients with mucolipidosis II and mucolipidosis III to agarose-immobilized concanavalin A revealed a two- to ten-fold decrease in the proportion of enzyme (that adsorbed On the lectin) [activities from patients with mucolipidoses II and III (see p. 424)1... 

The use of P. multicolor a-L-fucosidase to synthesise 2-acetamido-3-0-(a-L-fucopyranosyl)-2-deoxy-D-glucopyranose using dimethylsulfoxide as cosolvent [24] (Figure 12.9). 

---