I have found that human serum biotinidase, a sialylated N-glycoprotein enzyme, is regulated by glycochains. Asialo human serum biotinidase has been found to reduce the affinity or increase the Km to substrates as compared to the intact sialylated human serum biotinidase (our sadly unpublished important observation).
Furthermore, the externally addition of Ganglyosides into the reaction mixture also changes the biotinidase kinetics (also our and with Dr. Claudio De Felice (University of Siena, Siena, Italy) miserably unpublished observation).
Further, I have found that Amo (kcat/Km) of LEW rat-brain biotinidase is higher in the left cerebrum than the right cerebrum (please see the Fig. 1 of file; J Chrom B Rat BIN LIP Km), and this kinetic difference can not be explained by genetic theory at all.
Therefore, substrate specificity of the hydrophobic glycoprotein enzyme seems to be under the control of the glycochain structure of glycoprotein and glycochains of some species of Glycolipids which binds to hydrophobic biotinidase, and not to be under the control of the genes or the amino-acid sequences of proteins.
About the kinetic changes induced by glycosidases are published in files "Wide range of Biotin" and "JMBT Alopecia".
Interestingly, L-fucose of liver biotinidase seems to increase Kip value in cancer tissue, and increased Kip has been normalized by the addition of fucoidan and heparin (please see file; Anticancer Res). Therefore, I have happily found that the edible Japanese fucoidan (sulphated poly-L-fucose) can surely cure the hepatocellular carcinoma (HCC) within three days (please see file; HepG2 fucoidan).