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Literature summary for 3.2.1.28 extracted from

  • Mansure, J.J.; Silva, J.T.; Panek, A.D.
    Characterization of trehalase in Rhodotorula rubra (1992), Biochem. Int., 28, 693-700.
    View publication on PubMed
Search for more literature for 3.2.1.28

Activating Compound

Activating Compound Comment Organism Structure
additional information activation by cAMP-dependent protein kinase Rhodotorula mucilaginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8
-
 trehalose
-
 Rhodotorula mucilaginosa

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information bound to particulate fraction Rhodotorula mucilaginosa
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
trehalose + H2O Rhodotorula mucilaginosa the trehalase is strongly repressed by glucose and derepressed during growth on maltose, trehalose and glycerol. The enzyme may be present in a constitutive form without the requirement for a specific inducer D-glucose
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodotorula mucilaginosa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trehalose + H2O
-
 Rhodotorula mucilaginosa D-glucose
-
 ?
trehalose + H2O the trehalase is strongly repressed by glucose and derepressed during growth on maltose, trehalose and glycerol. The enzyme may be present in a constitutive form without the requirement for a specific inducer Rhodotorula mucilaginosa D-glucose
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Rhodotorula mucilaginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6
-
-
 Rhodotorula mucilaginosa