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Literature summary for 3.2.1.68 extracted from

  • Li, Y.; Zhang, L.; Ding, Z.; Gu, Z.; Shi, G.
    Engineering of isoamylase improvement of protein stability and catalytic efficiency through semi-rational design (2016), J. Ind. Microbiol. Biotechnol., 43, 3-12 .
    View publication on PubMed
Search for more literature for 3.2.1.68

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Lederbergia lentus

Protein Variants

Protein Variants Comment Organism
G608A the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme Lederbergia lentus
G608K the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme Lederbergia lentus
G608V the kcat/Km values of the mutant are promoted by 49% and the specific activity increases by 33% as compared to the wild type enzyme Lederbergia lentus
N513A the kcat/Km values of the mutant are slightly decreased and the specific activity is decreased as compared to the wild type enzyme Lederbergia lentus
N513K the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme Lederbergia lentus
N513V the kcat/Km values and the specific activity of the mutant are strongly decreased as compared to the wild type enzyme Lederbergia lentus
R505A the kcat/Km values of the mutant are promoted and the specific activity is decreased as compared to the wild type enzyme Lederbergia lentus
R505E the acidic stability is enhanced and the specific activity of the mutant is increased by 13% compared to the wild type enzyme Lederbergia lentus
R505P the thermal stability of the mutant is enhanced compared to the wild type enzyme Lederbergia lentus

Organism

Organism UniProt Comment Textmining
Lederbergia lentus
-
-
-
Lederbergia lentus JNU3
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap chelating column chromatography Lederbergia lentus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 1130 units/mg, mutant enzyme R505E, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus
additional information
-
 1326 units/mg, mutant enzyme G608V, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus
additional information
-
 232 units/mg, mutant enzyme N513V, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus
additional information
-
 475 units/mg, mutant enzyme G608K, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus
additional information
-
 487 units/mg, mutant enzyme N513K, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus
additional information
-
 614 units/mg, mutant enzyme N513A, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus
additional information
-
 642 units/mg, mutant enzyme R505A, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus
additional information
-
 677 units/mg, mutant enzyme G608A, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus
additional information
-
 801 units/mg, mutant enzyme R505P, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus
additional information
-
 995 units/mg, wild type enzyme, at pH 6.0 and 50°C. One unit of enzyme activity is defined as the amount of enzyme capable of resulting 0.01 increase in absorbance at 600 nm per h Lederbergia lentus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycogen + H2O
-
 Lederbergia lentus ?
-
 ?
glycogen + H2O
-
 Lederbergia lentus JNU3 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 100000, SDS-PAGE Lederbergia lentus

Synonyms

Synonyms Comment Organism
glycogen-6-glucanohydrolase
-
 Lederbergia lentus
IAM
-
 Lederbergia lentus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
 the wild type enzyme loses 50% of its initial activity after 1 h at 80°C Lederbergia lentus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
212
-
 glycogen mutant enzyme N513V, at pH 6.0 and 50°C Lederbergia lentus
286
-
 glycogen mutant enzyme N513K, at pH 6.0 and 50°C Lederbergia lentus
298
-
 glycogen mutant enzyme G608K, at pH 6.0 and 50°C Lederbergia lentus
433
-
 glycogen mutant enzyme G608A, at pH 6.0 and 50°C Lederbergia lentus
472
-
 glycogen mutant enzyme N513A, at pH 6.0 and 50°C Lederbergia lentus
510
-
 glycogen mutant enzyme R505A, at pH 6.0 and 50°C Lederbergia lentus
597
-
 glycogen mutant enzyme R505P, at pH 6.0 and 50°C Lederbergia lentus
660
-
 glycogen wild type enzyme, at pH 6.0 and 50°C Lederbergia lentus
890
-
 glycogen mutant enzyme R505E, at pH 6.0 and 50°C Lederbergia lentus
904
-
 glycogen mutant enzyme G608V, at pH 6.0 and 50°C Lederbergia lentus

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.5
-
 during 10 h incubation at pH 4.5 and 20°C, the activity of wild type enzyme rapidly declines with the increase of time until 35% of its initial activity is retained Lederbergia lentus