Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

Cbz-gplgp (2S)-1-[2-[[(2S)-4-methyl-2- [[(2S)-1-(2...

Synonyms: SureCN10627504, AR-1K3257, AC1L4W3B, AC1Q5R6R, C03183, ...

Auriault, C. et al., Ichishima, E. et al., Yamakawa, Y. et al.

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High impact information on Z-Gly-Pro-Leu-Gly-Pro

The purification of the schistosome proteases by preparative isoelectric focusing and gel filtration demonstrated that neutral proteases able to hydrolyze the collagenase substrates Azocoll and Z-Gly-Pro-Leu-Gly-Pro are able to significantly enhance eosinophil effector functions [1].
Aspergillus saitoi acid carboxypeptidase hydrolyzed C-terminal peptidyl-L-proline bonds and released the C-terminal proline from Z-Gly-Pro-Leu-Gly-Pro and Z-Gly-Pro at pH 3 [2].
It did not hydrolyze a peptide, Z-Gly-Pro-Leu-Gly-Pro, which had been a good substrate for the major proteinase in the venom [3].

References

Enhancement of eosinophil effector function by soluble factors released by S. mansoni: role of proteases. Auriault, C., Capron, M., Cesari, I.M., Capron, A. J. Immunol. (1983) [Pubmed]
C-Terminal peptidyl-L-proline hydrolase activity of Aspergillus acid carboxypeptidase. Ichishima, E., Takeuchi, M., Yasuda, R., Suzuki, Y., Kobayashi, S. J. Biochem. (1977) [Pubmed]
Purification, characterization and substrate specificity of a basic proteinase in the venom of habu (Trimeresurus flavoviridis). Yamakawa, Y., Omori-Satoh, T., Sadahiro, S. Biochim. Biophys. Acta (1987) [Pubmed]

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