16060-65-4Relevant articles and documents
The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity
Szeltner,Alshafee,Juhasz,Parvari,Polgar
, p. 2376 - 2381 (2005)
The PREPL (previously called KIAA0436) gene encodes a putative serine peptidase from the prolyl oligopeptidase family. A chromosomal deletion involving the PREPL gene leads to a severe syndrome with multiple symptoms. Homology with oligopeptidase B suggested that the enzyme cleaves after an arginine or lysine residue. Several PREPL splice variants have been identified, and a 638-residue variant (PREPL A) was expressed in Escherichia coli and purified. Its secondary structure was similar to that of oligopeptidase B, but differential-scanning calorimetry indicated a higher conformational stability. Dimerization may account for the enhanced stability. Unexpectedly, the PREPL A protein did not cleave peptide substrates containing a P1 basic residue, but did slowly hydrolyse an activated ester substrate, and reacted with diisopropyl fluorophosphate. These results indicated that the catalytic serine is a reactive residue. However, the negligible hydrolytic activity suggests that the function of PREPL A is different from that of the other members of the prolyl oligopeptidase family. Birkhaeuser Verlag, 2005.
Direct guanylation of amino groups by cyanamide in water: Catalytic generation and activation of unsubstituted carbodiimide by scandium(iii) triflate
Tsubokura, Kazuki,Iwata, Takayuki,Taichi, Misako,Kurbangalieva, Almira,Fukase, Koichi,Nakao, Yoichi,Tanaka, Katsunori
, p. 1302 - 1306 (2014/06/10)
Guanylation proceeded efficiently upon treatment of the various amines with cyanamide in the presence of catalytic amounts of scandium(III) triflate under mild conditions. The method did not require the guanylation reagents to be preactivated, and the reaction proceeded efficiently in water. The method, therefore, has practical utility for substrates that dissolve only in aqueous solutions, for example, peptides or pharmacologically important compounds. Georg Thieme Verlag Stuttgart New York.
Synthesis of 4-(4-guanidinobenzoyloxy)benzamides and 1-(4-guanidinobenzoyloxy)benzoyloxy acetamides as trypsin inhibitors
Zlatoidsky,Maliar
, p. 895 - 899 (2007/10/03)
Seventeen new compounds of 4-(4-guanidinobenzoyloxy)benzamides and 4-(4-guanidinobenzoyloxy)benzoyloxyacetamides were prepared and their inhibitory activities on trypsin, thrombin and porcine pancreatic elastase were measured. These compounds were found to be selective trypsin inhibitors with inhibiting activities from 0.44 to 43 μM.
