Cloned (Comment) | Organism |
---|---|
human cathepsins V expressed in Pichia pastoris | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
cystatin | cystatin inhibition relies on occlusion of the active site rather than the substrate-like behavior of serpins, unaltered by addition of DNA | Homo sapiens | |
serpin | cofactors fine tuning serpin activity in the extracellular milieu analyzed, DNA accelerate the rate at which the model serpin MENT inhibit cathepsin V up to 50-fold, primarily effected via the protease and secondarily by the recruitment of the DNA as a template onto which cathepsin V and MENT are bound, altered substrate turnover and conformational change within the protease observed, enzyme concentration constant at 0.1 nM, serpin concentration varying between 0.5 and 60 nM with a maximum of 5 nM serpin in the presence of DNA | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | presence of ds65-mer DNA causes a nonsignificant decrease in the Km value for the interaction between cathepsin V and the substrate, values from about 33.1 microM to 27.5 microM measured | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O60911 | - |
- |
Purification (Comment) | Organism |
---|---|
gel filtration, pre-activated before use | Homo sapiens |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
interaction between cathepsin V with the model serpins MENT and SCCA-1 and with cystatin A analyzed, association rate constant (ka) for cathepsin V interaction in the presence and absence of cofactors determined, stoichiometry of inhibition (SI) in the absence and presence of cofactors determined, kinetic parameters of MENT and cystatin A in the presence of various DNA constructs ranging between 18mers and 65mers measured, binding of serpins and cathepsin V to DNA indicated by gel mobility shift analysis, electrostatic potential of human cathepsins V and effect of dsDNA on cathepsin V fluorescence indicated | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O | mechanisms of interaction between serpins, human cathepsin V and DNA analyzed, kinetic constants for substrate cleavage in the presence and absence of cofactors determined, final concentrations of cathepsin V and ds65mer DNA at 0.1 and 10 nM, final substrate concentrations ranging from 5 to 200 microM in cathepsin V buffer | Homo sapiens | N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | presence of DNA reduces the turnover rate up to 50% indicating that the binding of DNA changes the active site of cathepsin V such that the enzyme interacts with peptide substrates differently | Homo sapiens |