Activating Compound | Comment | Organism | Structure |
---|---|---|---|
dithiothreitol | addition of dithiothreitol results in an increase in the branching enzyme activity up to 2.4fold at concentrations greater than 1 mM. This activation is not observed if idoacetamide is simultaneously present. | Anaerobranca gottschalkii |
Cloned (Comment) | Organism |
---|---|
the gene encoding the branching enzyme from Anaerobranca gottschalkii is fused with a twin arginine translocation protein secretory-pathway-dependent siganl sequence from Escherichia coli and expressed in Staphylococcus carnosus | Anaerobranca gottschalkii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | the additon of 2.5 mM of Ca2+ slightly inhibits the enzyme | Anaerobranca gottschalkii | |
Co2+ | the additon of 2.5 mM of Co2+ slightly inhibits the enzyme | Anaerobranca gottschalkii | |
EDTA | enzymatic activity is abolished in the presence of EDTA | Anaerobranca gottschalkii | |
Fe3+ | enzymatic activity is abolished in the presence of Fe3+ | Anaerobranca gottschalkii | |
Mg2+ | the additon of 2.5 mM of Mg2+ slightly inhibits the enzyme | Anaerobranca gottschalkii | |
Mn2+ | the additon of 2.5 mM of Mn2+ slightly inhibits the enzyme | Anaerobranca gottschalkii | |
Zn2+ | enzymatic activity is abolished in the presence of Zn2+ | Anaerobranca gottschalkii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
72000 | - |
SDS-PAGE and non-denaturing PAGE | Anaerobranca gottschalkii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Anaerobranca gottschalkii | Q3BJY5 | the protein consists of 613 amino acids. The branching enzyme of Anaerobranca gottschalkii lacks the N-terminal extension of approximately 100 amino acids found in the branching enzymes of Escherichia coli and its close phylogenetic relatives. The absence of a signal sequence indicates that the branching enzyme is an intracellular enzyme. | - |
Purification (Comment) | Organism |
---|---|
Phenyl Sepharose 6 Fast Flow column and Superdex 200 gel filtration column | Anaerobranca gottschalkii |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
the branching enzyme has a spesific activity of 0.4 U/mg. Amylose is used as substrate. The methods defines one unit of branching enzyme activity as 1 micromol of alpha-1,6 linkages synthesized per minute. | Anaerobranca gottschalkii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | cyclodextrins neither serve as donors nor as acceptors | Anaerobranca gottschalkii | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
the branching enzyme is optimally active at 50°C and pH 7 | Anaerobranca gottschalkii |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | 55 | in the absence of substrates the branching enzyme is stable at 50°C for more than 6 h. At 55°C the half-life of the branching enzyme is 50 min. | Anaerobranca gottschalkii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
the branching enzyme is optimally active at 50°C and pH 7 | Anaerobranca gottschalkii |