Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.16.5 extracted from

  • Sorensen, S.B.; Breddam, K.
    The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket (1997), Protein Sci., 6, 2227-2232.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
L267A kcat/Km of mutant enzyme in% of the of the wild-type value: 18.7% for furylacryloyl-Ala-Leu, 71.7% for furylacryloyl-Ala-Glu, 113% for furylacryloyl-Ala-Lys, 130% for furylacryloyl-Ala-Arg,10.8% for furylacryloyl-Phe-Ala, 18.5% for furylacryloyl-Phe-Val and 31.3% for furylacryloyl-Phe-Leu Saccharomyces cerevisiae
L267D mutation greatly reduces the activity towards hydrophobic P1' residues and increases the activity for the hydrolysis of substrates with Lys or Arg in P1' Saccharomyces cerevisiae
L267D/L272A
-
Saccharomyces cerevisiae
L267D/L272D mutant enzyme with a preference for substrates with C-terminal basic amino acid residues Saccharomyces cerevisiae
L267E mutation greatly reduces the activity towards hydrophobic P1' residues and increases the activity for the hydrolysis of substrates with Lys or Arg in P1' Saccharomyces cerevisiae
L267F kcat/Km of mutant enzyme in% of the of the wild-type value: 88.5% for furylacryloyl-Ala-Leu, 65.2% for furylacryloyl-Ala-Glu, 44% for furylacryloyl-Ala-Lys, 53% for furylacryloyl-Ala-Arg, 34.2% for furylacryloyl-Phe-Ala, 57.8% for furylacryloyl-Phe-Val and 82.6% for furylacryloyl-Phe-Leu Saccharomyces cerevisiae
L267K mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion Saccharomyces cerevisiae
L267Q kcat/Km of mutant enzyme in% of the of the wild-type value: 17% for furylacryloyl-Ala-Leu, 48% for furylacryloyl-Ala-Glu, 157% for furylacryloyl-Ala-Lys, 63% for furylacryloyl-Ala-Arg Saccharomyces cerevisiae
L267R mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion Saccharomyces cerevisiae
L272A kcat/Km of mutant enzyme in% of the of the wild-type value: 8.7% for furylacryloyl-Ala-Leu, 60.9% for furylacryloyl-Ala-Glu, 127% for furylacryloyl-Ala-Lys, 47% for furylacryloyl-Ala-Arg, 78.9% for furylacryloyl-Phe-Ala, 50% for furylacryloyl-Phe-Val and 15.6% for furylacryloyl-Phe-Leu Saccharomyces cerevisiae
L272D
-
Saccharomyces cerevisiae
L272E
-
Saccharomyces cerevisiae
L272F kcat/Km of mutant enzyme in% of the of the wild-type value: 83% for furylacryloyl-Ala-Leu, 95.7% for furylacryloyl-Ala-Glu, 46% for furylacryloyl-Ala-Lys, 63% for furylacryloyl-Ala-Arg, 113% for furylacryloyl-Phe-Ala, 121% for furylacryloyl-Phe-Val and 83.4% for furylacryloyl-Phe-Leu Saccharomyces cerevisiae
L272K mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion Saccharomyces cerevisiae
L272Q
-
Saccharomyces cerevisiae
L272R mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion Saccharomyces cerevisiae
L272R/M398F
-
Saccharomyces cerevisiae
L272R/T60F
-
Saccharomyces cerevisiae
S297A kcat/Km of mutant enzyme in% of the of the wild-type value: 39.7% for furylacryloyl-Ala-Leu, 161% for furylacryloyl-Ala-Glu, 66% for furylacryloyl-Ala-Lys, 80% for furylacryloyl-Ala-Arg, 126% for furylacryloyl-Phe-Ala, 109% for furylacryloyl-Phe-Val and 88.6% for furylacryloyl-Phe-Leu Saccharomyces cerevisiae
S297D
-
Saccharomyces cerevisiae
S297E
-
Saccharomyces cerevisiae
S297F kcat/Km of mutant enzyme in% of the of the wild-type value: 43.7% for furylacryloyl-Ala-Leu, 71.7% for furylacryloyl-Ala-Glu, 42% for furylacryloyl-Ala-Lys, 6.7% for furylacryloyl-Ala-Arg, 86.8% for furylacryloyl-Phe-Ala, 55% for furylacryloyl-Phe-Val and 60.9% for furylacryloyl-Phe-Leu Saccharomyces cerevisiae
S297K mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion Saccharomyces cerevisiae
S297Q
-
Saccharomyces cerevisiae
S297R mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion Saccharomyces cerevisiae
T60F/L267D/L272A
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation from Peptech, Hilleroed, Denmark Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
furylacryloyl-Ala-Arg + H2O
-
Saccharomyces cerevisiae furylacryloyl-Ala + Arg
-
?
furylacryloyl-Ala-Glu + H2O
-
Saccharomyces cerevisiae furylacryloyl-Ala + Glu
-
?
furylacryloyl-Ala-Leu + H2O
-
Saccharomyces cerevisiae furylacryloyl-Ala + Leu
-
?
furylacryloyl-Ala-Lys + H2O
-
Saccharomyces cerevisiae furylacryloyl-Ala + Lys
-
?
furylacryloyl-Phe-Ala + H2O
-
Saccharomyces cerevisiae furylacryloyl-Phe + Ala
-
?
furylacryloyl-Phe-Leu + H2O
-
Saccharomyces cerevisiae furylacryloyl-Phe + Leu
-
?
furylacryloyl-Phe-Val + H2O
-
Saccharomyces cerevisiae furylacryloyl-Phe + Val
-
?