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Chemical Compound Review: 

PZ-Plgpa     (2S)-5- (diaminomethylideneamino)-2- [[(2S)...

Synonyms: AC1L4830, 20283-89-0, PZ-Pro-leu-gly-prop-arg
 
 
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Disease relevance of PZ-Pro-leu-gly-prop-arg

  • Isolation and characterization of the Treponema denticola prtA gene coding for chymotrypsinlike protease activity and detection of a closely linked gene encoding PZ-PLGPA-hydrolyzing activity [1].
 

High impact information on PZ-Pro-leu-gly-prop-arg

  • The enzyme contains 1 mol of Zn/mol and the hydrolysis of PZ-PLGPA is slightly increased by Ca2+ [2].
  • The resultant protease positive clone NHS1, harboring plasmid pS1 with a 5.9-kilobase P. gingivalis insert, expressed an enzyme capable of hydrolyzing the synthetic collagenase substrate PZ-PLGPA as well as solubilized type I collagen [3].
  • In general, peptidase substrates and PZ-PLGPA were hydrolyzed at a higher rate by suspensions than by extracts, while protease substrates (such as casein) were hydrolyzed faster by the extracts [4].

References

  1. Isolation and characterization of the Treponema denticola prtA gene coding for chymotrypsinlike protease activity and detection of a closely linked gene encoding PZ-PLGPA-hydrolyzing activity. Que, X.C., Kuramitsu, H.K. Infect. Immun. (1990) [Pubmed]
  2. Purification and properties of an extracellular collagenolytic protease produced by the human oral bacterium Bacillus cereus (strain Soc 67). Makinen, K.K., Makinen, P.L. J. Biol. Chem. (1987) [Pubmed]
  3. Isolation and preliminary characterization of the Porphyromonas gingivalis prtC gene expressing collagenase activity. Takahashi, N., Kato, T., Kuramitsu, H.K. FEMS Microbiol. Lett. (1991) [Pubmed]
  4. Biochemical comparison of proteolytic enzymes present in rough- and smooth-surfaced capnocytophagas isolated from the subgingival plaque of periodontitis patients. Söderling, E., Mäkinen, P.L., Syed, S., Mäkinen, K.K. J. Periodont. Res. (1991) [Pubmed]
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