Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme is preferably inhibited by aspartate-based inhibitors | Saccharomyces cerevisiae | |
Z-VAD-fmk | i.e. carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone, a broad-spectrum caspase inhibitor, potent inhibition, binding structure determination and analysis with wild-type and mutant C191A enzyme, the inhibitor binds covalently to the catalytic residue Cys191, but not to the catalytic His218 | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Manalpha(1-6)(Xylbeta(1-2))Manbeta(1-4)GlcNAcbeta(1-4)(Fucalpha(1-3))GlcNAc-Asn-Asp-Glu-Ser-Ser + H2O = Manalpha(1-6)(Xylbeta(1-2))Manbeta(1-4)GlcNAcbeta(1-4)(Fucalpha(1-3))GlcNAc + Asn-Asp-Glu-Ser-Ser | the catalytic triad is formed by Cys191, His218, and Asp235 | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
peptide:N-glycanase | - |
Saccharomyces cerevisiae |
YPng1 | - |
Saccharomyces cerevisiae |