EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.21.4 | recombinant rat trypsinogen II is produced as an alpha-factor fusion protein in a Saccharomyces cerevisiae expression system from the pYT plasmid | Rattus norvegicus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.4.21.4 | C191A | mutation decreases the activity of trypsin by 20-200fold as measured by the ratio of turnover number to Km-value for the hydrolysis of amide substrates, ester hydrolysis is decreased by less than 10fold | Rattus norvegicus |
3.4.21.4 | C191A/C220A | the mutant enzyme binds bovine pancreatic trypsin inhibitor with the same affinity as trypsin, the affinity of benzamidine is decresed 10fold and the affinity of leupeptin is decreased 100fold | Rattus norvegicus |
3.4.21.4 | C220A | mutation decreases the activity of trypsin by 20-200fold as measured by the ratio of turnover number to Km-value for the hydrolysis of amide substrates, ester hydrolysis is decreased by less than 10fold | Rattus norvegicus |
3.4.21.4 | additional information | loss of the Cys191-Cys220 disulfide has no effect on the stability of trypsin as measured by urea denaturation | Rattus norvegicus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.4.21.4 | additional information | - |
additional information | the mutations C191A and C220A decrease the activity of trypsin by 20-200fold as measured by the ratio of turnover number to Km-value for the hydrolysis of amide substrates, ester hydrolysis is decreased by less than 10fold | Rattus norvegicus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.4 | Rattus norvegicus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.4 | benzyloxycarbonyl-Arg-thiobenzyl ester + H2O | - |
Rattus norvegicus | benzyloxycarbonyl-Arg + phenylmethanethiol | - |
? | |
3.4.21.4 | benzyloxycarbonyl-Lys-thiobenzyl ester + H2O | - |
Rattus norvegicus | benzyloxycarbonyl-Lys + phenylmethanethiol | - |
? | |
3.4.21.4 | D-Val-Leu-Arg-4-methylcoumarin 7-amide + H2O | - |
Rattus norvegicus | ? | - |
? | |
3.4.21.4 | D-Val-Leu-Lys-4-methylcoumarin 7-amide + H2O | - |
Rattus norvegicus | ? | - |
? | |
3.4.21.4 | D-Val-Leu-Lys-thiobenzyl ester + H2O | - |
Rattus norvegicus | ? | - |
? | |
3.4.21.4 | tosyl-Gly-Pro-Arg-4-methylcoumarin 7-amide + H2O | - |
Rattus norvegicus | ? | - |
? | |
3.4.21.4 | tosyl-Gly-Pro-Lys-4-methylcoumarin 7-amide + H2O | - |
Rattus norvegicus | ? | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.4.21.4 | additional information | - |
additional information | the mutations C191A and C220A decrease the activity of trypsin by 20-200fold as measured by the ratio of turnover number to Km-value for the hydrolysis of amide substrates, ester hydrolysis is decreased by less than 10fold | Rattus norvegicus |