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Literature summary extracted from

  • Cheng, Q.; Gao, H.; Hu, N.
    A trehalase from Zunongwangia sp. characterization and improving catalytic efficiency by directed evolution (2016), BMC Biotechnol., 16, 9 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.28 ADP 1 mM, activation to 139% of control Zunongwangia sp.
3.2.1.28 ATP 1 mM, activation to 156% of control Zunongwangia sp.
3.2.1.28 Ba2+ 10 mM, activation to 112% of control Zunongwangia sp.
3.2.1.28 Ni2+ 10 mM, activation to 113% of control Zunongwangia sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.28
-
 Zunongwangia sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.28 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 Zunongwangia sp.
3.2.1.28 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 Zunongwangia sp.
3.2.1.28 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) Zunongwangia sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.28 ADP 5 mM, 23% loss of activity Zunongwangia sp.
3.2.1.28 ATP 5 mM, 21% loss of activity Zunongwangia sp.
3.2.1.28 Co2+ 5 mM, 58% loss of activity Zunongwangia sp.
3.2.1.28 Cu2+ 5 mM, 96% loss of activity Zunongwangia sp.
3.2.1.28 EDTA 1 mM, 29% loss of activity Zunongwangia sp.
3.2.1.28 Fe3+ 5 mM, 34% loss of activity Zunongwangia sp.
3.2.1.28 K+ 10 mM, % loss of activity Zunongwangia sp.
3.2.1.28 Zn2+ 1 mM, 80% loss of activity Zunongwangia sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.28 0.3793
-
 alpha,alpha-trehalose mutant enzyme Y227H/R442G, 50°C, pH 6.0 Zunongwangia sp.
3.2.1.28 0.4317
-
 alpha,alpha-trehalose mutant enzyme R442G, 50°C, pH 6.5 Zunongwangia sp.
3.2.1.28 0.7194
-
 alpha,alpha-trehalose mutant enzyme Y227H, 50°C, pH 6.5 Zunongwangia sp.
3.2.1.28 0.99
-
 alpha,alpha-trehalose wild type enzyme, 50°C, pH 6.5 Zunongwangia sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.28 NaCl activity is increased by the presence of NaCl, showing the highest activity (136 %) at 1 M NaCl Zunongwangia sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.28 61300
-
 calculated from sequence Zunongwangia sp.

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.28 Zunongwangia sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.28
-
 Zunongwangia sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.28 alpha,alpha-trehalose + H2O
-
 Zunongwangia sp. beta-D-glucose + alpha-D-glucose
-
 ?
3.2.1.28 additional information no activity with sucrose, maltose, lactose or cellobiose Zunongwangia sp. ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.28 TreZ
-
 Zunongwangia sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.28 50
-
 wild type enzyme, mutant enzyme Y227H/R442G, mutant enzyme Y227H, mutant enzyme R442G Zunongwangia sp.

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.28 40 60 more than 50% of their original activities in the temperature range of 40 to 60 °C, wild type enzyme, mutant enzyme Y227H/R442G, mutant enzyme Y227H, mutant enzyme R442G Zunongwangia sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.28 263.25
-
 alpha,alpha-trehalose wild type enzyme, 50°C, pH 6.5 Zunongwangia sp.
3.2.1.28 299.83
-
 alpha,alpha-trehalose mutant enzyme Y227H, 50°C, pH 6.5 Zunongwangia sp.
3.2.1.28 319.88
-
 alpha,alpha-trehalose mutant enzyme R442G, 50°C, pH 6.5 Zunongwangia sp.
3.2.1.28 433.69
-
 alpha,alpha-trehalose mutant enzyme Y227H/R442G, 50°C, pH 6.0 Zunongwangia sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.28 6
-
 mutant enzyme Y227H/R442G Zunongwangia sp.
3.2.1.28 6.5
-
 wild type enzyme Zunongwangia sp.
3.2.1.28 6.5
-
 mutant enzyme R442G Zunongwangia sp.
3.2.1.28 6.5
-
 mutant enzyme Y227H Zunongwangia sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.28 5 8 retains more than 60% of the original activity in a pH range of 5.0-8.0, wild type enzyme, mutant enzyme Y227H/R442G, mutant enzyme Y227H, mutant enzyme R442G Zunongwangia sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.28 Zunongwangia sp. calculated from sequence
-
 4.98

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.28 265.91
-
 alpha,alpha-trehalose wild type enzyme, 50°C, pH 6.5 Zunongwangia sp.
3.2.1.28 416.78
-
 alpha,alpha-trehalose mutant enzyme Y227H, 50°C, pH 6.5 Zunongwangia sp.
3.2.1.28 740.97
-
 alpha,alpha-trehalose mutant enzyme R442G, 50°C, pH 6.5 Zunongwangia sp.
3.2.1.28 1143.4
-
 alpha,alpha-trehalose mutant enzyme Y227H/R442G, 50°C, pH 6.0 Zunongwangia sp.