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Literature summary extracted from

  • Shashidhara, K.S.; Gaikwad, S.M.
    Conformational and functional transitions in class II alpha-mannosidase from Aspergillus fischeri (2010), J. Fluoresc., 20, 827-836.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.2.1.114 unfolding and denaturation in 6 M guanidinium hydrochloride, the protein almost completely unfolds in 4.0 M guanidinium hydrochloride, overview Aspergillus fischeri

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.114 guanidinium hydrochloride the enzyme loses 54% and 70% of the original activity in 0.5 M and 1.0 M guanidinium hydrochloride, respectively. Irreversible denaturation at higher concentration of 6 M of guanidinium hydrochloride, kinetics, overview. The protein almost completely unfolds in 4.0 M guanidinium hydrochloride Aspergillus fischeri

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.114 Aspergillus fischeri
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.114 4-methylumbelliferyl alpha-D-mannopyranoside + H2O
-
 Aspergillus fischeri 4-methylumbelliferol + alpha-D-mannopyranose
-
 ?
3.2.1.114 4-nitrophenyl alpha-D-mannopyranoside + H2O
-
 Aspergillus fischeri 4-nitrophenol + alpha-D-mannopyranose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.114 class II alpha-mannosidase
-
 Aspergillus fischeri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.114 30
-
 assay at Aspergillus fischeri

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.114 30 90 activity is reduced by 8% at 50°C while positive ellipticity at 190-195 nm is almost same in the temperature range of 35-50°C. The activity is not affected in this range. At 60°C, 18% and at 70°C and above, 25% loss in the alpha-helical content of the protein occurs with significant decrease in the positive ellipticity, the protein does not completely unfold at 90°C Aspergillus fischeri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.114 6 6.5
-
 Aspergillus fischeri

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.114 additional information
-
 pH dependent denaturation, kinetics, overview Aspergillus fischeri
3.2.1.114 5 7 the enzyme is most stable, inactivation below pH 5.0 and above pH 8.0 is irreversible Aspergillus fischeri