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Literature summary extracted from

  • Van der Wilden, W.; Chrispeels, M.J.
    Characterization of the isoenzymes of alpha-mannosidase located in the cell wall, protein bodies, and endoplasmatic reticulum of Phaseolus vulgaris cotyledons (1983), Plant Physiol., 71, 82-87.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.24 cell wall isoforms III present Phaseolus vulgaris 5618
-
3.2.1.24 endoplasmic reticulum 3 isoforms present Phaseolus vulgaris 5783
-
3.2.1.24 protein storage vacuole isoforms I and II present Phaseolus vulgaris 326
-
3.2.1.24 protoplast isoforms I and II present Phaseolus vulgaris
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.24 Zn2+ 4 mM required for maximum activity Phaseolus vulgaris

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.24 Phaseolus vulgaris
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.24 cotyledon 3 isoforms, I, II and III Phaseolus vulgaris
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.24 p-nitrophenyl-alpha-D-mannopyranoside + H2O
-
Phaseolus vulgaris p-nitrophenol + alpha-D-mannopyranose
-
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pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.24 4.5
-
-
Phaseolus vulgaris

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.24 3.3 5.5 50% activity at pH 3.3 and pH 5.5 Phaseolus vulgaris