Literature DB >> 19038284

Class II alpha-mannosidase from Aspergillus fischeri: energetics of catalysis and inhibition.

K S Shashidhara1, Sushama M Gaikwad.   

Abstract

Energetics of the catalysis of Class II alpha-mannosidase (E.C.3.2.1.24) from Aspergillus fischeri was studied. The enzyme showed Kcat/Km for Man (alpha1-3) Man, Man (alpha1-2) Man and Man (alpha1-6) 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 alpha1-3, alpha1-2 and alpha1-6 linked mannobioses, respectively, reflecting the energy barrier in the hydrolysis of latter two substrates. The enzyme showed Kcat/Km as 3.56x10(5) and 4.61x10(5) M(-1) min(-1) and Ea as 38.7 and 8.92 kJ/mol, towards pNPalphaMan and 4-MeUmbalphaMan, respectively. Binding of Swainsonine to the enzyme is stronger than that of 1-deoxymannojirimycin.

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Year:  2008        PMID: 19038284     DOI: 10.1016/j.ijbiomac.2008.10.012

Source DB:  PubMed          Journal:  Int J Biol Macromol        ISSN: 0141-8130            Impact factor:   6.953


  2 in total

1.  Conformational and functional transitions in class II alpha-mannosidase from Aspergillus fischeri.

Authors:  K S Shashidhara; Sushama M Gaikwad
Journal:  J Fluoresc       Date:  2010-03-04       Impact factor: 2.217

2.  Sequential processing of mannose-containing glycans by two α-mannosidases from Solitalea canadensis.

Authors:  Fang F Liu; Anna Kulinich; Ya M Du; Li Liu; Josef Voglmeir
Journal:  Glycoconj J       Date:  2016-02-11       Impact factor: 2.916

  2 in total

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