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Literature summary for 3.2.1.10 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

Inhibitors Comment Organism Structure
(-)-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
isofagomine stereoisomer of (-)-1-azafagomine, racemic, competitive Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
isomaltase
-
Saccharomyces cerevisiae

Ki Value [mM]

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