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Literature summary for 2.4.1.18 extracted from

  • Thiemann, V.; Saake, B.; Vollstedt, A.; Schaefer, T.; Puls, J.; Bertoldo, C.; Freudl, R.; Antranikian, G.
    Heterologous expression and characterization of a novel branching enzyme from the thermoalkaliphilic anaerobic bacterium Anaerobranca gottschalkii (2006), Appl. Microbiol. Biotechnol., 72, 60-71.
    View publication on PubMed
Search for more literature for 2.4.1.18

Activating Compound

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(Commentary)

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

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 [Da] Molecular Weight Maximum [Da] Comment Organism
72000
-
 SDS-PAGE and non-denaturing PAGE Anaerobranca gottschalkii

Organism

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 (Commentary)

Purification (Comment) Organism
Phenyl Sepharose 6 Fast Flow column and Superdex 200 gel filtration column Anaerobranca gottschalkii

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 the branching enzyme is optimally active at 50°C and pH 7 Anaerobranca gottschalkii

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 the branching enzyme is optimally active at 50°C and pH 7 Anaerobranca gottschalkii