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Literature summary extracted from

  • van Assche, J.A.; Carlier, A.R.
    Some properties of trehalase from Phycomyces blakesleeanus (1975), Biochim. Biophys. Acta, 391, 154-161.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.28 additional information
-
 additional information trehalase from dormant spores shows a deviation from the Michaelis-Menten equation Phycomyces blakesleeanus
3.2.1.28 55
-
 trehalose trehalase from activated spores Phycomyces blakesleeanus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.28 210000
-
 enzyme from activated spores and from dormant spores, gel filtration Phycomyces blakesleeanus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.28 Phycomyces blakesleeanus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.28 spore contains 2 different forms which are convertible in vivo: a form with low activity found in dormant spores and an active form after breaking the dormancy Phycomyces blakesleeanus
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.28 36
-
 90 min, 93.3% loss of activity of the enzyme from activated spores, 67% loss of activity of the enzyme from dormant spores Phycomyces blakesleeanus