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Literature summary for 2.4.1.18 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
Search for more literature for 2.4.1.18

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aquifex aeolicus

Localization

Localization Comment Organism GeneOntology No. Textmining
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

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
85
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 soluble and insoluble enzyme form, stable up to Aquifex aeolicus

pH Optimum

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