20488-28-2Relevant articles and documents
Synthesis of Prolylproline
Gaidukevich,Popova,Zubreichuk,Knizhnikov
, p. 1005 - 1008 (2019/09/03)
Prolylproline has been synthesized by both classical peptide synthesis method utilizing tert-butoxycarbonyl or trifluoroacetyl protection of the NH group and carbodiimide-promoted peptide bond formation and by opening of the dioxopiperazine ring in octahydrodipyrrolo[1,2-a:1′,2′-d]pyrazine-5,10-dione obtained by thermolysis of proline methyl ester.
Functional identification and structure determination of two novel prolidases from cog1228 in the amidohydrolase superfamily
Xiang, Dao Feng,Patskovsky, Yury,Xu, Chengfu,Fedorov, Alexander A.,Fedorov, Elena V.,Sisco, Abby A.,Sauder, J. Michael,Burley, Stephen K.,Almo, Steven C.,Raushel, Frank M.
experimental part, p. 6791 - 6803 (2011/05/05)
Two uncharacterized enzymes from the amidohydrolase superfamily belonging to cog1228 were cloned, expressed, and purified to homogeneity. The two proteins, Sgx9260c (gi|44242006) and Sgx9260b (gi|44479596), were derived from environmental DNA samples originating from the Sargasso Sea. The catalytic function and substrate profiles for Sgx9260c and Sgx9260b were determined using a comprehensive library of dipeptides and N-acyl derivative of l-amino acids. Sgx9260c catalyzes the hydrolysis of Gly-l-Pro, l-Ala-l-Pro, and N-acyl derivatives of l-Pro. The best substrate identified to date is N-acetyl-l-Pro with a value of kcat/Km of 3 × 105 M -1 s-1. Sgx9260b catalyzes the hydrolysis of l-hydrophobic l-Pro dipeptides and N-acyl derivatives of l-Pro. The best substrate identified to date is N-propionyl-l-Pro with a value of kcat/Km of 1 × 105 M-1 s-1. Three-dimensional structures of both proteins were determined by X-ray diffraction methods (PDB codes 3MKV and 3FEQ). These proteins fold as distorted (β/α) 8-barrels with two divalent cations in the active site. The structure of Sgx9260c was also determined as a complex with the N-methylphosphonate derivative of l-Pro (PDB code 3N2C). In this structure the phosphonate moiety bridges the binuclear metal center, and one oxygen atom interacts with His-140. The α-carboxylate of the inhibitor interacts with Tyr-231. The proline side chain occupies a small substrate binding cavity formed by residues contributed from the loop that follows β-strand 7 within the (β/α)8-barrel. A total of 38 other proteins from cog1228 are predicted to have the same substrate profile based on conservation of the substrate binding residues. The structure of an evolutionarily related protein, Cc2672 from Caulobacter crecentus, was determined as a complex with the N-methylphosphonate derivative of l-arginine (PDB code 3MTW).
STUDIES OF BITTER PEPTIDES FROM CASEIN HYDROLYZATE - VII. BITTERNESS OF THE RETRO-BPIa (VAL-ILE-PHE-PRO-PRO-GLY-ARG) AND ITS FRAGMENTS.
Shigenaga,Otagiri,Kanehisa,Okai
, p. 103 - 107 (2007/10/02)
To explain the bitter taste exhibited by BPIa (Arg-Gly-Pro-Pro-Phe-Ile-Val) which was isolated from casein hydrolyzate, the authors propose the following requirement: its characteristic spatial structure: the basic moiety in the N-terminal and the hydroph
Studies on Peptides. CXV. Synthesis of Hylambatin, a New Frog Skin Peptide of the Kassinin Family
Okamoto, Kenji,Yasumura, Koichi,Fujitani, Kazuyoshi,Katakura, Shinichi,Akaji, Kenichi,et al.
, p. 430 - 437 (2007/10/02)
Hylambatin, a dodecapeptide amide isolated from the skin of an African rhacopharid frog (Hylambates maculatus), was synthesized by two routes, by successive condensations of four fragments, i.e., (1-3), (4-5), (6-10), and (11-12) in one case and (1-3), (4
