Crystallization (Comment) | Organism |
---|---|
enzyme in apoform and in complex with mannopentaose, the precipitant solution contains 25% w/v PEG 3350, 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis, modelling | Cryptopygus antarcticus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cryptopygus antarcticus | B4XC07 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
mannopentaose + H2O | - |
Cryptopygus antarcticus | mannose + mannotetraose | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme adopts a TIM (beta/alpha)8-barrel fold | Cryptopygus antarcticus |
Synonyms | Comment | Organism |
---|---|---|
beta-1,4-D-mannanase | - |
Cryptopygus antarcticus |
CaMan | - |
Cryptopygus antarcticus |
cold-adapted beta-mannanase | - |
Cryptopygus antarcticus |
endo-beta-1,4-D-mannanase | - |
Cryptopygus antarcticus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
cold-adapted beta-mannanase | Cryptopygus antarcticus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
- |
60 | the enzyme shows 20-40% of its maximum activity at 0-4°C and has its optimum at 30°C, about 10% of maximal activity at 50-60°C, inactivation at 70°C, profile overview | Cryptopygus antarcticus |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the glycosyl hydrolae famiyl 5, GH5 | Cryptopygus antarcticus |
additional information | the enzyme has an extended loop that alters topography of the active site, structural and mutational analyses, overview. The extended loop is linked to the cold-adapted enzymatic activity, structure of mannose-recognition subsites. Glu181 and Glu312 are highly conserved catalytic residues, Glu181 is the catalytic acid/base, and Glu312 is the nucleophile. Trp341, which is located in the vicinity of the catalytic residues, acts as a hydrophobic platform for sugar binding in catalytic site, the enzyme also has a second mannan binding site. Sequence comparisons, overview | Cryptopygus antarcticus |