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Literature summary extracted from

  • Londesborough, J.; Varimo, K.
    Characterization of two trehalases in baker's yeast (1984), Biochem. J., 219, 511-518.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.28 MgATP2- C-trehalase can be activated by MgATP2- in presence of cAMP Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.28 acetate strong inhibition by acetic acid/acetate buffer, V-trehalase Saccharomyces cerevisiae
3.2.1.28 EDTA 1 mM, C-trehalase, complete inhibition Saccharomyces cerevisiae
3.2.1.28 K+ 100 mM KCl, 65% inhibition of C-trehalase Saccharomyces cerevisiae
3.2.1.28 MgCl2 50 mM, C-trehalase, complete inhibition Saccharomyces cerevisiae
3.2.1.28 ZnCl2 0.1 mM, C-trehalase, complete inhibition Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.28 1.4
-
 trehalose V-trehalase Saccharomyces cerevisiae
3.2.1.28 5.7
-
 trehalose C-trehalase Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.28 Ca2+ C-trehalase is absolutely dependent on Ca2+ or Mn2+. 4fold activation of C-trehalase at 2.5 mM CaCl2 Saccharomyces cerevisiae
3.2.1.28 K+ 30% activation by 100 mM KCl, V-trehalase Saccharomyces cerevisiae
3.2.1.28 Mn2+ 30% activation by 20-300 mM neutral salts such as KCl, NaNO3 and MnCl2, V-trehalase. C-trehalase is absolutely dependent on Ca2+ or Mn2+. 2fold activation of C-trehalase by MnCl2 Saccharomyces cerevisiae
3.2.1.28 Na+ 30% activation by 20-300 mM neutral salts such as KCl, NaNO3 and MnCl2, V-trehalase Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.28 170000
-
 C-trehalase, gel filtration Saccharomyces cerevisiae
3.2.1.28 215000
-
 V-trehalase, gel filtration Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.28 Saccharomyces cerevisiae
-
 two enzyme activities, C-trehalase and V-trehalase
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.28 trehalose + H2O
-
 Saccharomyces cerevisiae D-glucose
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.28 4 5 V-trehalase, at 40 mM trehalose Saccharomyces cerevisiae
3.2.1.28 6.7
-
 at 40 mM trehalose, C-trehalase Saccharomyces cerevisiae