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3.2.1.28: alpha,alpha-trehalase

This is an abbreviated version!
For detailed information about alpha,alpha-trehalase, go to the full flat file.

Word Map on EC 3.2.1.28

Reaction

alpha,alpha-trehalose
+
H2O
=
beta-D-glucose
 +
alpha-D-glucose

Synonyms

acid (non regulatory) trehalase, acid non-regulatory trehalase, acid trehalase, alkaline trehalase, alpha,alpha glucoside 1-glucohydrolase, alpha,alpha trehalase, alpha,alpha trehalose glucohydrolase, alpha,alpha'-trehalose 1-D-glucohydrolase, Alpha,alpha-trehalase, Alpha,alpha-trehalose glucohydrolase, alpha-glucoside-1-glucohydrolase, ATC1, Atc1p, Ath1, ATHA, ATM1, GH37 trehalase, glucose alpha-1,1-glucose hydrolase, HaTre-1, HaTreh-1, Hl-Tre, membrane-bound SfTre2, MSMEG 4528, neutral regulatory trehalase, neutral trehalase, NT-INV, Ntc1p, NTH1, Nth1p, Nth2p, NTHA, Ntp1p, Px_EclTre, Saci_1816, SeTre-1, SeTre-2, SfTre1, soluble P I type trehalase, soluble P II type trehalase, soluble trehalase, THA, Tre-2, TRE1, Tre37A, TreA, treB, TreF, Treh, Treh1, Treh2, trehalase, trehalase-1, trehalase-invertase, TreZ

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.28 alpha,alpha-trehalase

Engineering

Engineering on EC 3.2.1.28 - alpha,alpha-trehalase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D108K
-
mutant enzyme fails to bind Ca2+ or to undergo enzyme activation
D97L
-
mutant enzyme fails to bind Ca2+ or to undergo enzyme activation
D322A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
E520A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis. In presence of azide, activity increases three fold
R169A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
R222A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
R222A/R287A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
R287A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
R442G
-
the mutant enzyme displays a 56% decrease in Km, a 22% increase in kcat, and a 1.78fold increase in kcat/Km compared with the wild type enzyme. The mutation reduces the size of the side chain and decreases the steric hindrance, which contributes to channel the substrate into the active cavity easier and promote the release of the product
Y227H
-
the mutant enzyme displays a 27% decrease in Km, a 14% increase in kcat, and a 0.57fold increase in kcat/Km compared with the wild type enzyme. The mutation enlarges the shape of the binding pocket, to improve the binding of the substrate and the release of the products
Y227H/R442G
-
the mutant enzyme displays a 61% decrease in Km, a 65% increase in kcat and a 3.3 fold increase in catalytic efficiency compared with the wild type enzyme (265.91 mmol-1 s-1)
additional information