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Literature summary for 3.2.1.24 extracted from

  • Snaith, S.M.
    Characterization of jack-bean alpha-D-mannosidase as a zinc metalloenzyme (1975), Biochem. J., 147, 83-90.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ nearly complete inhibition at 0.005 mM Canavalia ensiformis
EDTA addition of Zn2+ restores inhibitory effect; strong inhibition at 1 mM Canavalia ensiformis

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains 2 mol Zn/mol enzyme Canavalia ensiformis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
230000
-
gel filtration Canavalia ensiformis

Organism

Organism UniProt Comment Textmining
Canavalia ensiformis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity, chromatography steps Canavalia ensiformis

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
Canavalia ensiformis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
45
-
in the presence of Zn2+ Canavalia ensiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-nitrophenyl-alpha-D-mannopyranoside + H2O
-
Canavalia ensiformis p-nitrophenol + alpha-D-mannopyranose
-
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