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Literature summary extracted from

  • Ong, P.C.; McGowan, S.; Pearce, M.C.; Irving, J.A.; Kan, W.T.; Grigoryev, S.A.; Turk, B.; Silverman, G.A.; Brix, K.; Bottomley, S.P.; Whisstock, J.C.; Pike, R.N.
    DNA accelerates the inhibition of human cathepsin V by serpins (2007), J. Biol. Chem., 282, 36980-36986.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.22.43 human cathepsins V expressed in Pichia pastoris Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.43 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
3.4.22.43 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.22.43 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

EC Number Organism UniProt Comment Textmining
3.4.22.43 Homo sapiens O60911
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Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.22.43 gel filtration, pre-activated before use Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.22.43 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.43 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
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Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.22.43 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