The specificity of two proteinases that cleave adjacent to arginine, C1 esterase and acrosin, for peptide p-nitroanilide substrates - PubMed (original) (raw)
The specificity of two proteinases that cleave adjacent to arginine, C1 esterase and acrosin, for peptide p-nitroanilide substrates
M T Skoog et al. Biochim Biophys Acta. 1989.
Abstract
Relative values of Vmax/Km for hydrolysis of 40 peptide p-nitroanilides catalyzed by human Cl-s and human acrosin are reported. For Cl-s, Ac-Lys(gamma Cbz)-Gly-Arg is the optimum sequence, but 25% of the substrates have (Vmax/Km)rel greater than 0.25 compared to this sequence. The best acrosin substrate tested has the sequence Tos-Gly-Pro-Arg, although (Vmax/Km)rel greater than 0.15 for more than half of the substrates. Proline at P2 is preferred by acrosin. Both enzymes prefer arginine at P1 greater than or equal to 3-fold over lysine and will not accept citrulline. In addition, occupancy of site S3 may yield an increase in Vmax/Km of greater than or equal to 10-fold with either enzyme, but many residues are accepted at S2, S3 and S4. Thus, an acrosin assay using Tos-Gly-Pro-Arg p-nitroanilide as a substrate is more than 20-times as sensitive as existing assays with blocked arginine derivatives.
Similar articles
- The complement component C1s catalysed hydrolysis of peptide 4-nitroanilide substrates.
Keogh SJ, Harding DR, Hardman MJ. Keogh SJ, et al. Biochim Biophys Acta. 1987 May 27;913(1):39-44. doi: 10.1016/0167-4838(87)90229-9. Biochim Biophys Acta. 1987. PMID: 3495295 - Human complement proteins D, C2, and B. Active site mapping with peptide thioester substrates.
Kam CM, McRae BJ, Harper JW, Niemann MA, Volanakis JE, Powers JC. Kam CM, et al. J Biol Chem. 1987 Mar 15;262(8):3444-51. J Biol Chem. 1987. PMID: 3546307 - Substrate specificity of ascidian sperm trypsin-like proteases, spermosin and acrosin.
Sawada H, Someno T. Sawada H, et al. Mol Reprod Dev. 1996 Oct;45(2):240-3. doi: 10.1002/(SICI)1098-2795(199610)45:2<240::AID-MRD18>3.0.CO;2-4. Mol Reprod Dev. 1996. PMID: 8914083 - Kinetic characterization of rat tissue kallikrein using N alpha-substituted arginine 4-nitroanilides and N alpha-benzoyl-L-arginine ethyl ester as substrates.
Sousa MO, Rodrigues CV, Pena HB, Alvarenga MG, Machado-Coelho GL, Santoro MM, Juliano MA, Juliano L, Figueiredo AF. Sousa MO, et al. Braz J Med Biol Res. 1996 Mar;29(3):327-34. Braz J Med Biol Res. 1996. PMID: 8736125
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources