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Literature summary for 2.4.1.10 extracted from

  • Xu, W.; Peng, J.; Zhang, W.; Zhang, T.; Guang, C.; Mu, W.
    Enhancement of the Brenneria sp. levansucrase thermostability by site-directed mutagenesis at Glu404 located at the -TEAP- residue motif (2019), J. Biotechnol., 290, 1-9 .
    View publication on PubMed
Search for more literature for 2.4.1.10

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Brenneria sp. EniD312

Protein Variants

Protein Variants Comment Organism
E404A the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404C the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404D the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404F the mutant exhibits an enhanced thermostability and the melting temperature of the mutant is enhanced by 1.5°C compared to the wild type enzyme Brenneria sp. EniD312
E404G the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404H the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404I the mutant exhibits an enhanced thermostability and and the melting temperature of the mutant is enhanced by 1.5°C compared to the wild type enzyme Brenneria sp. EniD312
E404K the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404L the melting temperature of the mutant is enhanced by 2.8°C and the half-life is increased by 12.5 and 1.3fold at 35 and 45°C, respectively, as compared to the wild type enzyme Brenneria sp. EniD312
E404M the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404N the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404P the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404Q the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404R the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404S the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404T the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312
E404V the mutant exhibits an enhanced thermostability and the melting temperature of the mutant is enhanced by 1.4°C compared to the wild type enzyme Brenneria sp. EniD312
E404W the mutant exhibits an enhanced thermostability and and the melting temperature of the mutant is enhanced by 1.6°C compared to the wild type enzyme Brenneria sp. EniD312
E404Y the mutant exhibits a decreased thermostability compared to the wild type enzyme Brenneria sp. EniD312

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
118
-
 sucrose mutant enzyme E404K, at pH 6.5 and 45°C Brenneria sp. EniD312
249
-
 sucrose mutant enzyme E404P, at pH 6.5 and 45°C Brenneria sp. EniD312
273
-
 sucrose mutant enzyme E404M, at pH 6.5 and 45°C Brenneria sp. EniD312
283
-
 sucrose mutant enzyme E404Q, at pH 6.5 and 45°C Brenneria sp. EniD312
284
-
 sucrose mutant enzyme E404F, at pH 6.5 and 45°C Brenneria sp. EniD312
286
-
 sucrose mutant enzyme E404H, at pH 6.5 and 45°C Brenneria sp. EniD312
287
-
 sucrose mutant enzyme E404Y, at pH 6.5 and 45°C Brenneria sp. EniD312
293
-
 sucrose mutant enzyme E404G, at pH 6.5 and 45°C Brenneria sp. EniD312
294
-
 sucrose mutant enzyme E404W, at pH 6.5 and 45°C Brenneria sp. EniD312
296
-
 sucrose mutant enzyme E404L, at pH 6.5 and 45°C Brenneria sp. EniD312
296
-
 sucrose mutant enzyme E404N, at pH 6.5 and 45°C Brenneria sp. EniD312
296
-
 sucrose mutant enzyme E404S, at pH 6.5 and 45°C Brenneria sp. EniD312
305
-
 sucrose wild type enzyme, at pH 6.5 and 45°C Brenneria sp. EniD312
309
-
 sucrose mutant enzyme E404V, at pH 6.5 and 45°C Brenneria sp. EniD312
318
-
 sucrose mutant enzyme E404I, at pH 6.5 and 45°C Brenneria sp. EniD312
338
-
 sucrose mutant enzyme E404T, at pH 6.5 and 45°C Brenneria sp. EniD312
346
-
 sucrose mutant enzyme E404D, at pH 6.5 and 45°C Brenneria sp. EniD312
355
-
 sucrose mutant enzyme E404A, at pH 6.5 and 45°C Brenneria sp. EniD312
370
-
 sucrose mutant enzyme E404C, at pH 6.5 and 45°C Brenneria sp. EniD312
377
-
 sucrose mutant enzyme E404R, at pH 6.5 and 45°C Brenneria sp. EniD312

Organism

Organism UniProt Comment Textmining
Brenneria sp. EniD312 G7LSK3
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-chelating affinity column chromatography Brenneria sp. EniD312

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + H2O
-
 Brenneria sp. EniD312 D-glucose + D-fructose
-
 ?
sucrose + sucrose
-
 Brenneria sp. EniD312 D-glucose + levan
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Brenneria sp. EniD312

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 55 more than 70% activity between 30 and 55°C Brenneria sp. EniD312

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35 55 the half-life of the wild type enzyme at 35, 45 and 55°C is 4.6 h, 2.1 h and 46 min, respectively. After incubation of 0.5, 1, 2, 4 and 6 h at 35°C, the wild type enzyme retains about 86, 65, 62, 58 and 38% activity, respectively. After incubation of 0.5, 1, 2, 4 and 6 h at 45°C, the wild type enzyme retains about 78, 55, 48, 28 and 12% activity, respectively. The melting temperature is 50°C Brenneria sp. EniD312

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Brenneria sp. EniD312

pH Range

pH Minimum pH Maximum Comment Organism
5.5 8.5 more than 50% activity between pH 5.5 and 8.5 Brenneria sp. EniD312