Crystallization (Comment) | Organism |
---|---|
Kex2 in complex with the Ac-R-E-R-K-chloromethylketone, containing a noncognate lysine at the P1 position. Secondary subsite in the S1 pocket is present, which recognizes and binds the P1 lysine in a more shallow fashion than arginine. Kex2 contains well defined subsites that have optimally arranged electrostatic charge that positions correct substrates for hydrolysis. Chemical nature of the peptidyl inhibitor has little effect on ligand positioning at the active site in the alkylated enzyme forms | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ac-R-E-R-K-chloromethylketone | alternate binding site and resultant displacement of the scissile bond in the active site results in a decrease in the acylation rate | Saccharomyces cerevisiae | |
decanoyl-R-V-K-R-chloromethylketone | - |
Saccharomyces cerevisiae | |
decanoyl-R-V-R-K-chloromethylketone | - |
Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
Kex2 | - |
Saccharomyces cerevisiae |
kexin | - |
Saccharomyces cerevisiae |
proprotein convertase Kex2 | - |
Saccharomyces cerevisiae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00019 | - |
decanoyl-R-V-K-R-chloromethylketone | - |
Saccharomyces cerevisiae | |
0.00845 | - |
decanoyl-R-V-R-K-chloromethylketone | - |
Saccharomyces cerevisiae |