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Results 1 - 5 of 5
EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.43-999 - expression of cathepsin V studied by RT-PCR and immunohistochemistry, cathepsin activity in aortic valves quantified by fluorometric microassay, increased mRNA expression and high activity of cathepsin V in stenotic valves observed, association of cathepsin V and the inhibitor cystatin C with calcific aortic valve disease determined, participation in adverse extracellular matrix remodelling of stenotic aortic valves suggested 683107
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.43-999 - expression of cathepsin V studied by RT-PCR and immunohistochemistry, cathepsin activity quantified by fluorometric microassay, intense association of cathepsin V with neovessels of the stenotic aortic valves reveals a role in neovascularization of the valves 683107
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.43-999 - inhibition properties of cathepsin V propeptide by fluorimetric assay determined, purification and expression of cathepsin V propeptide described, recombinant cathepsin V used for inhibition studies 683207
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.43-999 - 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 683662
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.43-999 - plasminogen digestion by cathepsin V determined by SDS-PAGE and by subsequent plasmin activity tests, sequences EKKVYL, TEQLAP and LLPNVE obtained by N-terminal sequencing compatible with cleavage sites at plasminogen F94-E95, S358-T359 and V468-L469 peptide bonds, in vitro angiogenesis Matrigel assay described, angiogenesis inhibition activity caused by plasminogen processing by cathepsin V determined 683210
Results 1 - 5 of 5