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Literature summary for 3.4.16.5 extracted from

  • Stennicke, H.R.; Mortensen, U.H.; Breddam, K.
    Studies on the hydrolytic properties of (serine) carboxypeptidase Y (1996), Biochemistry, 35, 7131-7141.
    View publication on PubMed
Search for more literature for 3.4.16.5

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Saccharomyces cerevisiae
0.16
-
 Furylacryloyl-Phe-OGly-OH wild-type Saccharomyces cerevisiae
0.41
-
 benzyloxycarbonyl-Phe-Glu furylacryloyl-Phe-Gly-OH Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 carboxypeptidase Y
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation Carlbiotech, Copenhagen, Denmark Saccharomyces cerevisiae
-
commercial preparation wild type and mutant enzyme Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
furylacryloyl-Phe ethyl ester + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
furylacryloyl-Phe-Gly + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
furylacryloyl-Phe-Leu + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
furylacryloyl-Phe-NHEt + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
furylacryloyl-Phe-OGly + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
furylacryloyl-Phe-OGly-OH + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
additional information studies on hydrolytic properties Saccharomyces cerevisiae ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Saccharomyces cerevisiae
24.2
-
 Furylacryloyl-Phe-OGly-OH wild-type enzyme Saccharomyces cerevisiae
61.7
-
 Furylacryloyl-Phe-OGly-OH wild-type enzyme Saccharomyces cerevisiae
68.3
-
 Furylacryloyl-Phe ethyl ester wild-type enzyme Saccharomyces cerevisiae