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Literature summary for 2.4.1.4 extracted from

  • Chin, Y.; Jang, S.; Shin, H.; Kim, T.; Kim, S.; Park, C.; Seo, D.
    Heterologous expression of Deinococcus geothermalis amylosucrase in Corynebacterium glutamicum for luteolin glucoside production (2020), Enzyme Microb. Technol., 135, 109505 .
    View publication on PubMed

Application

Application Comment Organism
industry the enzyme has great industrial potential owing to its multifunctional activities, including transglucosylation, polymerization, and isomerization Deinococcus geothermalis

Cloned(Commentary)

Cloned (Comment) Organism
heterologous expression of Deinococcus geothermalis amylosucrase in Corynebacterium glutamicum Deinococcus geothermalis

Organism

Organism UniProt Comment Textmining
Deinococcus geothermalis Q1J0W0
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Deinococcus geothermalis DSM 11300 Q1J0W0
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-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA chromatography Deinococcus geothermalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information luteolin transglucosylation activity in Corynebacterium glutamicum amylosucrase (cDGAS) is 10% higher than that in the Corynebacterium glutamicum enzyme expressed in Escherichia coli (eDGAS) Deinococcus geothermalis ?
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additional information luteolin transglucosylation activity in Corynebacterium glutamicum amylosucrase (cDGAS) is 10% higher than that in the Corynebacterium glutamicum enzyme expressed in Escherichia coli (eDGAS) Deinococcus geothermalis DSM 11300 ?
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Synonyms

Synonyms Comment Organism
ASASE
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Deinococcus geothermalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
Deinococcus geothermalis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65.19
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melting temperature Deinococcus geothermalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Deinococcus geothermalis