02163nas a2200253   4500008004100000022001400041245013100055210006900186260011700255300001000372490000600382520116900388653001601557653002201573653002601595653002701621653001501648100002401663700002001687700002601707700003101733700001501764856013001779       2009                        eng d  a0973-626300aInteraction of alpha-mannosidase from aspergillus fischeri with glycosidase inhibitors, metal ions and group specific reagents0 aInteraction of alphamannosidase from aspergillus fischeri with g  aSECTOR A-80, SCHEME NO 54, VIJAY NAGAR, A B ROAD, INDORE, 452 010 MP, INDIAbRESEARCH JOURNAL BIOTECHNOLOGYcNOV  a39-480 v43 a<p>As an initial step towards using alpha-mannosidase as a target against anticancer drugs, inhibition studies of a model enzyme, class II alpha-mannosidase from Aspergillus fischeri in presence of polyhydroxy piperidine derived glycosidase inhibitors, metal ions and amino acid specific reagents were carried out to reveal the sensitivity of the enzyme. Three of the derivatives (Compound 20, 32 and 39)(11) showed competitive inhibition (K(i) =45, 48 and 235 mu M) and the binding of the inhibitors to the enzyme was entropically driven. Among the metal ions checked, Cu(++) (K(i) = 21nm) and Se(++) ions (K(i) = 32 mu M) showed noncompetitive and Co(++) (K(i) = 1.195 mM) showed competitive inhibition of the enzyme activity with insignificant change in the secondary structure of the protein. The above studies exhibit the Potential of the enzyme in studying anticancer drugs. Treatment of the enzyme with group specific reagents showed the presence of carboxylate, Arg and Cys at the active site. Substrate protection studies and kinetics of the modified enzyme confirmed the above results. Trp and His at the active site were observed to be in proximity.</p>10aactive-site10aalpha-Mannosidase10aChemical modification10aGlycosidase inhibitors10ametal ions1 aShashidhara, K., S.1 aGaikwad, S., M.1 aKhan, Mohammad, Islam1 aBharadwaj, Kishor, Chandra1 aPandey, G.  uhttps://library.ncl.res.in/content/interaction-alpha-mannosidase-aspergillus-fischeri-glycosidase-inhibitors-metal-ions-and-0