@article { ISI:000262769700020, title = {Class II alpha-mannosidase from aspergillus fischeri: energetics of catalysis and inhibition}, journal = {International Journal of Biological Macromolecules}, volume = {44}, number = {1}, year = {2009}, month = {JAN}, pages = {112-115}, publisher = {ELSEVIER SCIENCE BV}, address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}, abstract = {

Energetics of the catalysis of Class II alpha-mannosidase (E.C.3.2.1.24) from Aspergillus fischeri was studied. The enzyme showed K(cat)/K(m) for Man (alpha 1-3) Man, Man (alpha 1-2) Man and Man (alpha 1-6) Man as 7488, 5376 and 3690 M(-1) min(-1), respectively. The activation energy, Ea was 15.14, 47.43 and 71.21 kJ/mol for a1-3, alpha 1-2 and alpha 1-6 linked mannobioses, respectively, reflecting the energy barrier in the hydrolysis of latter two substrates. The enzyme showed K(cat)/K(m) as 3.56 x 10(5) and 4.61 x 10(5) M(-1) min(-1) and E(a) as 38.7 and 8.92 kJ/mol, towards pNP alpha Man and 4-MeUmb alpha Man, respectively. Binding of Swainsonine to the enzyme is stronger than that of 1-deoxymannojirimycin. (C) 2008 Elsevier B.V. All rights reserved.

}, keywords = {alpha-Mannosidase, Energy of activation, kinetics, Swainsonine}, issn = {0141-8130}, doi = {10.1016/j.ijbiomac.2008.10.012}, author = {Shashidhara, K. S. and Gaikwad, Sushama M.} }