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Literature summary extracted from

  • Takata, H.; Ohdan, K.; Takaha, T.; Kuriki, T.; Okada, S.
    Properties of branching enzyme from hyperthermophilic bacterium, Aquifex aeolicus, and its potential for production of highly-branched cyclic dextrin (2003), J. Appl. Glycosci., 50, 15-20.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18 expression in Escherichia coli Aquifex aeolicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.18 additional information more than 95% of the recombinant enzyme is present within the cells as insoluble but catalytically active aggregate. Heat treatment of the aggregate suspension at 70°C results in about 30% solubilization of the enzyme activity Aquifex aeolicus
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Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Aquifex aeolicus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.18 amylopectin the enzyme cyclizes the B-chain which connects the cluster structures of amylopectin. The product, highly branched cyclic dextrin, has a ring structure with DPw 50 and non-cyclic chains with an average unit chain length of 16 connected to the ring Aquifex aeolicus amylopectin with additional alpha-1,6-glucosidic linkages
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Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.18 75
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soluble and insoluble enzyme form Aquifex aeolicus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.18 70
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pH 7.0, 30 min, 10% loss of the soluble enzyme form, 50% loss of the insoluble enzyme form Aquifex aeolicus
2.4.1.18 85
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soluble and insoluble enzyme form, stable up to Aquifex aeolicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.18 7.5 8 soluble and insoluble enzyme form Aquifex aeolicus