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Literature summary extracted from

  • Dellamora-Ortiz, G.M.; Ortiz, C.H.D.; Maia, J.C.C.; Panek, A.D.
    Partial purification and characterization of the interconvertible forms of trehalase from Saccharomyces cerevisiae (1986), Arch. Biochem. Biophys., 251, 205-214.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.28 4.79
-
 trehalose in absence of trehalose-c Saccharomyces cerevisiae
3.2.1.28 5.28
-
 trehalose in presence of trehalose-c Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.28 160000
-
 gel filtration Saccharomyces cerevisiae

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.28 side-chain modification multiple forms of cryptic totally inactive trehalase-c of 32000 Da, 160000 Da and 80000 Da are activated by protein kinase. A single active enzyme form, trehalase-a of 16000 Da is formed Saccharomyces cerevisiae

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.28 partial Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
3.2.1.28 4°C, 0.02 M phosphate buffer, pH 6.2, the cryptic trehalase-c is completely stable in dilute aqueous solution and can be activated even after 6 months Saccharomyces cerevisiae
3.2.1.28 4°C, pH 7.5, 20% glycerol, 20% loss of activity of trehalase-a after 5 months Saccharomyces cerevisiae

Substrates and Products (Substrate)

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