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Literature summary 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

EC Number Protein Variants Comment Organism
3.4.16.5 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
3.4.16.5 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
3.4.16.5 L267D/L272A
-
 Saccharomyces cerevisiae
3.4.16.5 L267D/L272D mutant enzyme with a preference for substrates with C-terminal basic amino acid residues Saccharomyces cerevisiae
3.4.16.5 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
3.4.16.5 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
3.4.16.5 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
3.4.16.5 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
3.4.16.5 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
3.4.16.5 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
3.4.16.5 L272D
-
 Saccharomyces cerevisiae
3.4.16.5 L272E
-
 Saccharomyces cerevisiae
3.4.16.5 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
3.4.16.5 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
3.4.16.5 L272Q
-
 Saccharomyces cerevisiae
3.4.16.5 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
3.4.16.5 L272R/M398F
-
 Saccharomyces cerevisiae
3.4.16.5 L272R/T60F
-
 Saccharomyces cerevisiae
3.4.16.5 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
3.4.16.5 S297D
-
 Saccharomyces cerevisiae
3.4.16.5 S297E
-
 Saccharomyces cerevisiae
3.4.16.5 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
3.4.16.5 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
3.4.16.5 S297Q
-
 Saccharomyces cerevisiae
3.4.16.5 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
3.4.16.5 T60F/L267D/L272A
-
 Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.5 Saccharomyces cerevisiae
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

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