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Literature summary for 2.4.1.18 extracted from

  • Wang, Z.; Xin, C.; Li, C.; Gu, Z.; Cheng, L.; Hong, Y.; Ban, X.; Li, Z.
    Expression and characterization of an extremely thermophilic 1,4-alpha-glucan branching enzyme from Rhodothermus obamensis STB05 (2019), Protein Expr. Purif., 164, 105478 .
    View publication on PubMed
Search for more literature for 2.4.1.18

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Rhodothermus marinus

General Stability

General Stability Organism
the enzyme shows higher activity in sodium citrate buffer than sodium phosphate buffer at pH 6.0 and higher activity in sodium phosphate buffer than glycine buffer at pH 8.0 Rhodothermus marinus

Inhibitors

Inhibitors Comment Organism Structure
Ba2+ 1 mM slightly reduces the enzyme activity (by approximately 10%) Rhodothermus marinus
Ca2+ 1 mM slightly reduces the enzyme activity (by approximately 10%) Rhodothermus marinus
Cu2+ 36.54% inhibition at 1 mM Rhodothermus marinus
EDTA the enzyme retains 73.39%, 39.01%, 19.06%, 7.64%, and 3.30% of its activity in the presence of 1, 2, 4, 8, and 10 mM EDTA, respectively Rhodothermus marinus
Fe3+ 17.33% inhibition at 1 mM Rhodothermus marinus
Mg2+ 1 mM slightly reduces the enzyme activity (by approximately 10%) Rhodothermus marinus
Zn2+ 1 mM slightly reduces the enzyme activity (by approximately 10%) Rhodothermus marinus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ Ca2+ does not promote the activity of purified enzyme, but may be required for its activity Rhodothermus marinus
additional information addition of Li+, Na+ or K+ has almost no effect on enzyme activity Rhodothermus marinus

Organism

Organism UniProt Comment Textmining
Rhodothermus marinus
-
-
-
Rhodothermus marinus STB05
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA resin chelating column chromatography Rhodothermus marinus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
potato amylopectin type III 100% activity Rhodothermus marinus potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
 ?
potato amylopectin type III 100% activity Rhodothermus marinus STB05 potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
 ?
potato amylose 65.4% activity compared to potato amylopectin type III Rhodothermus marinus potato amylose containing alpha-1,6-glucosidic linkages
-
 ?
potato amylose 65.4% activity compared to potato amylopectin type III Rhodothermus marinus STB05 potato amylose containing alpha-1,6-glucosidic linkages
-
 ?
soluble starch 47.3% activity compared to potato amylopectin type III Rhodothermus marinus soluble starch containing alpha-1,6-glucosidic linkages
-
 ?
soluble starch 47.3% activity compared to potato amylopectin type III Rhodothermus marinus STB05 soluble starch containing alpha-1,6-glucosidic linkages
-
 ?
tapioca starch 46.5% activity compared to potato amylopectin type III Rhodothermus marinus tapioca starch containing alpha-1,6-glucosidic linkages
-
 ?
tapioca starch 46.5% activity compared to potato amylopectin type III Rhodothermus marinus STB05 tapioca starch containing alpha-1,6-glucosidic linkages
-
 ?
waxy corn starch 74.7% activity compared to potato amylopectin type III Rhodothermus marinus waxy corn starch containing alpha-1,6-glucosidic linkages
-
 ?
waxy corn starch 74.7% activity compared to potato amylopectin type III Rhodothermus marinus STB05 waxy corn starch containing alpha-1,6-glucosidic linkages
-
 ?

Subunits

Subunits Comment Organism
? x * 73000, SDS-PAGE Rhodothermus marinus
? x * 73200, calculated from amino acid sequence Rhodothermus marinus

Synonyms

Synonyms Comment Organism
GBE
-
 Rhodothermus marinus
glycogen branching enzyme
-
 Rhodothermus marinus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
 Rhodothermus marinus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 80 the enzyme has more than 60% activity between 50 and 80°C, 93.85% of maximal activity at 60°C, and 95.61% of maximal activity at 70°C Rhodothermus marinus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70 90 the enzyme remains stable at temperatures up to 80°C and has a half-life at 85°C of approximately 31 min. The enzyme is quite stable (for at least 2 h) at 70°C or lower, and 92% of the initial enzyme activity is retained at 80°C for 2 h. Furthermore, the enzyme demonstrates half-lives at 85 and 90°C of 31 min and 2.5 min, respectively Rhodothermus marinus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Rhodothermus marinus

pH Range

pH Minimum pH Maximum Comment Organism
5.5 7.5 the enzyme shows at least 80% of maximal activity from pH 5.5 to pH 7.5. The enzyme activity decreases rapidly at pH values lower than 5.5 and higher than 9.0 Rhodothermus marinus

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 11 the enzyme has broad pH stability between pH 3.0 and 11.0 at 4°C, and prefers weakly acidic conditions at high temperatures (85°C). More than 96% of the initial enzyme activity is retained after incubation at pH 3.0-11.0 for 1 h. The enzyme loses all activity when incubated for 15 min at pH 3.0 or 4.0, and its half-life is 14.9 min at pH 5.0. The enzyme retains 72.1% of its initial activity after 1 h at pH 6.0 in sodium citrate buffer Rhodothermus marinus