Literature summary for 2.4.1.18 extracted from

Feng, L.; Fawaz, R.; Hovde, S.; Gilbert, L.; Chiou, J.; Geiger, J.H.
Crystal structures of Escherichia coli branching enzyme in complex with linear oligosaccharides (2015), Biochemistry, 54, 6207-6218.

Search for more literature for 2.4.1.18

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of truncated branching enzyme mutant DELTA112 in complex with linear oligosaccharides maltoheptaose and maltohexaose, X-ray diffraction structure determination and analysis	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P07762	-	-

Subunits

Subunits	Comment	Organism
More	six distinct oligosaccharide binding sites on the surface of the branching enzyme, most of which surround the edge of the beta-barrel domain and are quite far from the active site	Escherichia coli

Synonyms

Synonyms	Comment	Organism
branching enzyme	-	Escherichia coli

General Information

General Information	Comment	Organism
evolution	the branching enzyme is an unusual member of the alpha-amylase family because it has both alpha-1,4-amylase activity and alpha-1,6-transferase activity	Escherichia coli
malfunction	mutations of conserved residues in binding sites I and VI have a debilitating effect on the activity of the enzyme	Escherichia coli
additional information	six distinct oligosaccharide binding sites on the surface of the branching enzyme, most of which surround the edge of the beta-barrel domain and are quite far from the active site. No evidence of oligosaccharide binding in the active site of the enzyme, the closest bound oligosaccharide resides almost 18 A from the active site	Escherichia coli
physiological function	the branching enzyme is responsible for all branching of glycogen and starch. It has both alpha-1,4-amylase activity and alpha-1,6-transferase activity	Escherichia coli

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Release 2023.1 (January 2023)