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Literature summary extracted from

  • Lohse, A.; Hardlei, T.; Jensen, A.; Plesner, I.W.; Bols, M.
    Investigation of the slow inhibition of almond beta-glucosidase and yeast isomaltase by 1-azasugar inhibitors: evidence for the 'direct binding' model (2000), Biochem. J., 349, 211-215.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.10 (-)-1-azafagomine i.e.(3R,4R,5R)-4,5-dihydroxy-3-hydroxymethylhexahydropyridazine, competitive, slow inhibition process, difference in Ki values depend almost entirely on changes in the binding rate constant, direct binding model, some analogues of the compound are also inhibitory with less efficiency Saccharomyces cerevisiae
3.2.1.10 isofagomine stereoisomer of (-)-1-azafagomine, racemic, competitive Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.10 Saccharomyces cerevisiae
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.10 commercial preparation partially purified Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.10 4-nitrophenyl alpha-D-glucopyranoside + H2O
-
 Saccharomyces cerevisiae 4-nitrophenol + alpha-D-glucopyranose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.10 isomaltase
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.10 additional information
-
 additional information inhibition kinetics Saccharomyces cerevisiae
3.2.1.10 0.00027
-
 (-)-1-azafagomine pH 6.8, 25°C Saccharomyces cerevisiae
3.2.1.10 0.0058
-
 isofagomine pH 6.8, 25°C Saccharomyces cerevisiae