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Literature summary for 3.2.1.114 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)

Crystallization (Comment) Organism
hanging drop vapor diffusion Drosophila melanogaster

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster Q24451
-
-

Synonyms

Synonyms Comment Organism
GmII
-
Drosophila melanogaster
Golgi alpha-mannosidase II
-
Drosophila melanogaster

Temperature Optimum [°C]

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

pH Optimum

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

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
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