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Literature summary extracted from

  • Kuntz, D.A.; Ghavami, A.; Johnston, B.D.; Pinto, B.M.; Rose, D.R.
    Crystallographic analysis of the interactions of Drosophila melanogaster Golgi alpha-mannosidase II with the naturally occurring glycomimetic salacinol and its analogues (2005), Tetrahedron Asymmetry, 16, 25-32.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.114 hanging drop vapor diffusion Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.114 diastereomer of salacinol
-
 Drosophila melanogaster
3.2.1.114 diastereomer of seleno-salacinol
-
 Drosophila melanogaster
3.2.1.114 ghavamiol
-
 Drosophila melanogaster
3.2.1.114 salacinol
-
 Drosophila melanogaster
3.2.1.114 seleno-salacinol
-
 Drosophila melanogaster
3.2.1.114 swainsonine
-
 Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.114 Drosophila melanogaster Q24451
-
-

Synonyms

EC Number Synonyms Comment Organism
3.2.1.114 GmII
-
 Drosophila melanogaster
3.2.1.114 Golgi alpha-mannosidase II
-
 Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.114 37
-
-
 Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.114 5.75
-
 in MES buffer Drosophila melanogaster

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.114 additional information
-
 additional information although too weak for full Ki analyses with the amounts of material available, all analogues with salacinol-like stereochemistry at positions 2 and 3 proved to be weak inhibitors of the enzyme with IC50 values of approximately 7.5 mM Drosophila melanogaster