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