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Literature summary for 2.4.1.19 extracted from

  • Goh, P.; Illias, R.; Goh, K.
    Domain replacement to elucidate the role of B domain in CGTase thermostability and activity (2012), Process Biochem., 47, 2123-2130.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
additional information replacement of B domain by corresponding domain from Thermococcus kodakarensis, Anaerobacter gottschalkii and Pyrococcus furiosus leads to complete loss of catalytic function. Replacement of B domain by corresponding domain from Bacillus stearothermophilus ET1 enzyme leads to a mutant protein with retained activity. The mutant has the wild-type temperature optimum of 60°C with increase in half-life to 57 min. Introduction of mutation F188Y to the mutant results in a half-life of 28 min at 60°C. Bith mutant strains display improved ability to form cyclodextrin and a faster turnover rate Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria) Q5U9V9
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Bacillus sp. (in: Bacteria) G1 Q5U9V9
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Synonyms

Synonyms Comment Organism
CGTase
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Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
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half-life 22 min for wild-type, 57 min for mutant carrying B domain from Bacillus stearothermophilus ET1 Bacillus sp. (in: Bacteria)