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Literature summary for 3.4.16.5 extracted from

  • Hahm, M.S.; Chung, B.H.
    Refolding and purification of yeast carboxypeptidase Y expressed as inclusion bodies in Escherichia coli (2001), Protein Expr. Purif., 22, 101-107.
    View publication on PubMed

Cloned(Commentary)

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

Localization Comment Organism GeneOntology No. Textmining
inclusion body recombinant enzyme expressed in Escherichia coli Saccharomyces cerevisiae 16234
-

Molecular Weight [Da]

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

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 (Commentary)

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 (Commentary)

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 [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-(2-furanacryloyl)-Phe-Phe + H2O
-
Saccharomyces cerevisiae N-(2-furanacryloyl)-Phe + Phe
-
?

Subunits

Subunits Comment Organism
? x * 61000, SDS-PAGE Saccharomyces cerevisiae
? x * 47000, recombinant enzyme, SDS-PAGE Saccharomyces cerevisiae