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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P07762 | - |
- |
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 | Comment | Organism |
---|---|---|
branching enzyme | - |
Escherichia coli |
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 |