Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli. The native enzyme is a glycoprotein whereas the recombinant enzyme produced from Escherichia coli is not glycosylated | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
inclusion body | recombinant enzyme expressed in Escherichia coli | Saccharomyces cerevisiae | 16234 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
47000 | - |
x * 47000, recombinant enzyme, SDS-PAGE | Saccharomyces cerevisiae |
61000 | - |
x * 61000, SDS-PAGE | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | the native enzyme is a glycoprotein whereas the recombinant enzyme produced from Escherichia coli is not glycosylated. The glycosylation does not greatly affect the enzymatic activity. Glycosylation is required for efficient intracellular transport of the enzyme but not for vacuolar sorting, in vivo stability or activity | Saccharomyces cerevisiae |
Purification (Comment) | Organism |
---|---|
development of a novel method that can produce active yeast enzyme from inactive inclusion bodies expressed in escherichia coli | Saccharomyces cerevisiae |
Renatured (Comment) | Organism |
---|---|
the denatured His-tagged carboxypeptidase propeptide is refolded by dilution 1:60 into the renaturation buffer, 50 mM Tris-HCl containing 0.5 M NaCl and 3 mM EDTA, pH 8.0. The denatured carboxypeptidase is refolded by dilution 1:60 into the reanturation buffer containing containing His-tagged carboxypeptidase propeptide at various concentrations. Increasing the molar ratio of His-tagged carboxypeptidase propeptide to carboxypeptidase results in an increase in the carboxypeptidase refolding yield, indicating that the His-tagged carboxypeptidase propeptide plays a chaperone-like role in in vitro folding of the carboxypeptidase. When refolding is carried out in the presence of 10 molar equivalent His-tagged carboxypeptidase propeptide the specific activity, N-(2-furanacryloyl)-Phe-Phe hydrolysis activity per mg of protein, is 63% of that of the native enzyme | Saccharomyces cerevisiae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-(2-furanacryloyl)-Phe-Phe + H2O | - |
Saccharomyces cerevisiae | N-(2-furanacryloyl)-Phe + Phe | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 61000, SDS-PAGE | Saccharomyces cerevisiae |
? | x * 47000, recombinant enzyme, SDS-PAGE | Saccharomyces cerevisiae |