Literature summary for 3.2.1.28 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.

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KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
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)

Purification (Comment)	Organism
partial	Saccharomyces cerevisiae

Storage Stability

Storage Stability	Organism
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
4°C, pH 7.5, 20% glycerol, 20% loss of activity of trehalase-a after 5 months	Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)