Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mannostatin A is a metabolite produced by the microorganism Streptoverticillium verticillus and reported to be a potent competitive inhibitor of rat epididymal alpha-mannosidase. When tested against a number of other arylglycosidases, mannostatin A was inactive toward alpha- and beta-glucosidase and galactosidase as well as beta-mannosidase, but it was a potent inhibitor of jack bean, mung bean, and rat liver lysosomal alpha-mannosidases, with estimated IC50's of 70 nM, 450 nM, and 160 nM, respectively. The type of inhibition was competitive in nature. This compound also proved to be an effective competitive inhibitor of the glycoprotein-processing enzyme mannosidase II (IC50 of about 10-15 nM with p-nitrophenyl alpha-D-mannopyranoside as substrate, and about 90 nM with [3H]mannose-labeled GlcNAc-Man5GlcNAc as substrate). However, it was virtually inactive toward mannosidase I. The N-acetylated derivative of mannostatin A had no inhibitory activity. In cell culture studies, mannostatin A also proved to be a potent inhibitor of glycoprotein processing. Thus, in influenza virus infected Madin Darby canine kidney (MDCK) cells, mannostatin A blocked the normal formation of complex types of oligosaccharides on the viral glycoproteins and caused the accumulation of hybrid types of oligosaccharides. This observation is in keeping with other data which indicate that the site of action of mannostatin A is mannosidase II. Thus, mannostatin A represents the first nonalkaloidal processing inhibitor and adds to the growing list of chemical structures that can have important biological activity.
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PMID:Mannostatin A, a new glycoprotein-processing inhibitor. 227 38

The glycosidase activities (beta-D-mannosidase, alpha-L-fucosidase and N-acetyl-beta-D-glucosaminidase) have been compared in whole and split ejaculate samples from men whose couple suffers from infertility. The site of secretion of enzymatic activities is either prostatic or epididymal. The three enzymatic activities have possibly different origin and should constitute new biochemical markers of male genital tract.
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PMID:On some glycosidases (beta-D-mannosidase, alpha-L-fucosidase, N-acetyl-beta-D-glucosaminidase) of human seminal plasma. 281 47

In this study specific activities of four acid glycosidases: beta-N-acethylhexosaminidase (beta-HEX), beta-galactosidase (beta-GAL), alpha- and beta-mannosidase (alpha- and beta-MAN) were investigated in Japanese quail testes and epididymides during posthatch development and regression after light reduction. The specific activity of testicular beta-HEX and beta-GAL increased steadily during posthatch development and assumed maximum values for testes weighing 200-400 mg, when numerous spermatocytes appear in the testes of quail, and then decreased slowly. These enzymes showed much higher specific activity after 15 days of light reduction, and decreased to the control level after 30 days. Activity of alpha- and beta-MAN remained rather constant during testicular development and involution. The epididymal activity of the acid glycosidases was very low in immature individuals, whereas in sexually mature birds it was found to increase several-fold. Short photoperiod resulted in a decreased activity of these enzymes after 30 days to the values found in immature birds. A marked increase in the activity of acid glycosidases in the epididymides of sexually mature animals and a decrease in this activity during epididymidal regression indicate that these enzymes take part in reproductive processes. It is concluded that the activities of beta-HEX, beta-GAL, alpha- and beta-MAN in the development and regression of Japanese quail testes and epididymides change similarly as in mammals.
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PMID:Changes in the activity of acid glycosidases during posthatch development and regression after light reduction of Japanese quail testes and epididymides. 1721 59