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Chemical Compound Review:

Dppacmk (2S)-N-[(2R)-2-amino-3- phenyl-propanoyl]-2...

Synonyms: FFRCK, Phe-phe-arg-CK, KST-1A8203, AR-1A2692, FT-0667798, ...

Potempa, J. et al., Persson, E. et al., Petersen, L.C.

Persson, Nielsen, Olsen,

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High impact information on Dppacmk

Met306Asp-FVIIa binds soluble TF with a dissociation constant of 13 nM (about 3-fold higher than that of FVIIa), and, in sharp contrast to FVIIa, its binding kinetics are unaltered after inactivation with D-Phe-Phe-Arg chloromethyl ketone [1].
Recombinant FVIIa is converted into a catalytically inert protein by reactive site residues reacting with Phe-Phe-Arg-chloromethyl ketone [2].

Associations of Dppacmk with other chemical compounds

This inhibitor, together with the peptidyl chloromethanes, D-Phe-Pro-Arg-CH2Cl and D-Phe-Phe-Arg-CH2Cl, which reacted most rapidly with the Arg-specific proteinases, could be used to active site titrate purified forms of the enzymes and enzymes found in crude fractions such as intact P. gingivalis cells, vesicles or membrane fractions [3].

References

Substitution of aspartic acid for methionine-306 in factor VIIa abolishes the allosteric linkage between the active site and the binding interface with tissue factor. Persson, E., Nielsen, L.S., Olsen, O.H. Biochemistry (2001) [Pubmed]
Active site-inhibited seven: mechanism of action including signal transduction. Petersen, L.C. Semin. Hematol. (2001) [Pubmed]
Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes. Potempa, J., Pike, R., Travis, J. Biol. Chem. (1997) [Pubmed]

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