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Literature summary for 3.2.1.28 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
Search for more literature for 3.2.1.28

Activating Compound

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

Cloned(Commentary)

Cloned (Comment) Organism
-
 Zunongwangia sp.

Protein Variants

Protein Variants Comment Organism
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.
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.
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

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Zunongwangia sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Zunongwangia sp.

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
TreZ
-
 Zunongwangia sp.

Temperature Optimum [°C]

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

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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

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

kcat/KM [mM/s]

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