Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Bacillus amyloliquefaciens |
Crystallization (Comment) | Organism |
---|---|
analysis of the copper active site | Bacillus amyloliquefaciens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | Cu(II) binds with KD value 43 nM at pH 5. The coordination geometry around the copper is distorted from axial symmetry | Bacillus amyloliquefaciens | |
Zn2+ | may substitue for Cu2+. KD value 0.0081 mM at pH 5 | Bacillus amyloliquefaciens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus amyloliquefaciens | - |
- |
- |
Bacillus amyloliquefaciens DSM 7 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
improved expression and purification protocol using Champion pET-SUMO vector, yielding high purity AA10 with yields in excess of 9 mg of protein per litre of culture | Bacillus amyloliquefaciens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-chitin + acceptor + O2 | - |
Bacillus amyloliquefaciens | oligosaccharide aldonic acids + reduced acceptor + H2O | - |
? | |
alpha-chitin + acceptor + O2 | - |
Bacillus amyloliquefaciens DSM 7 | oligosaccharide aldonic acids + reduced acceptor + H2O | - |
? | |
beta-chitin + acceptor + O2 | beta chitin from squid pen, best substrate | Bacillus amyloliquefaciens | oligosaccharide aldonic acids + reduced acceptor + H2O | strong preference towards even-numbered products | ? | |
beta-chitin + acceptor + O2 | beta chitin from squid pen, best substrate | Bacillus amyloliquefaciens DSM 7 | oligosaccharide aldonic acids + reduced acceptor + H2O | strong preference towards even-numbered products | ? |
Synonyms | Comment | Organism |
---|---|---|
AA10 | - |
Bacillus amyloliquefaciens |
RBAM17540 | - |
Bacillus amyloliquefaciens |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
chitin binding increases the thermal stability of the enzyme by 8.3 degrees, copper binding increases melting temperature by 21.6 degrees. Addition of chitin to the copper-bound enzyme increases thermal stability by additional 3.5 degrees | Bacillus amyloliquefaciens |
68.7 | - |
melting temperature, presence of both copper and chitin | Bacillus amyloliquefaciens |