3.4.22.43: cathepsin V
This is an abbreviated version!
For detailed information about cathepsin V, go to the full flat file.
Word Map on EC 3.4.22.43
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3.4.22.43
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cathepsins
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papain-like
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elastases
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elastolytic
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legumain
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l-like
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medicine
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diagnostics
- 3.4.22.43
- cathepsins
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papain-like
- elastases
-
elastolytic
- legumain
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l-like
- medicine
- diagnostics
Reaction
The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec) =
Synonyms
cathepsin L2, cathepsin L2/V, cathepsin like 2, cathepsin U, cathepsin V, cathepsin V/L2, cathepsin-V, CatV, CL2, CTSL2, CTSV, CV/L2, hcatV, More, stratum corneum thiol protease
ECTree
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Specific Activity
Specific Activity on EC 3.4.22.43 - cathepsin V
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additional information
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
additional information
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
additional information
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
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
additional information
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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
additional information
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
additional information
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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