Literature summary for 2.4.1.18 extracted from

Hilden, I.; Leggio, L.L.; Larsen, S.; Poulsen, P.
Characterization and crystallization of an active N-terminally truncated form of the Escherichia coli glycogen branching enzyme (2000), Eur. J. Biochem., 267, 2150-2155.

Search for more literature for 2.4.1.18

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli, full-length enzyme and a truncated enzyme form missing the first 107 amino acids	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop method, active N-terminally truncated form missing the first 107 amino acids	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
truncated enzyme form missing the first 107 amino-	the purified full-length enzyme is poorly soluble and forms aggregates, which are inactive, at concentrations above 1 mg/ml. In contrast, the truncated form can be concentrated to 6 mg/ml without a visible signs of aggregation or loss of activity on concentration	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
soluble	the purified full-length enzyme is poorly soluble and forms aggregates, which are inactive, at concentrations above 1 mg/ml. In contrast, the truncated form can be concentrated to 6 mg/ml without a visible sign of aggregation or loss of activity on concentration	Escherichia coli	-	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Escherichia coli	the enzyme is responsible for the formation of the alpha-1,6 linkages in the glycogen molecule	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme is responsible for the formation of the alpha-1,6 linkages in the glycogen molecule	Escherichia coli	?	-	?

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Release 2023.1 (January 2023)