1118-90-7Relevant articles and documents
Hydrolytic cleavage of pyroglutamyl-peptide bond. I. The susceptibility of pyroglutamyl-peptide bond to dilute hydrochloric acid
Hashimoto,Ohki,Sakura
, p. 2068 - 2074 (1995)
The susceptibility of the pyroglutamyl-peptide bond in some biologically active peptides, dog neuromedin U-8 fragment (pGlu-Phe-Leu-Phe-Arg-Pro-Arg- OH), human big gastrin fragment (pGlu-Leu-Gly-Pro-OH) and thyrotropin releasing hormone (TRH) fragments (pGlu-His-Pro-OH, pGlu-His-OH), to 1 N HCl under mild conditions and/or at 60°C was studied. It was found that the N- terminal portion of pGlu-peptides is extremely labile to acid hydrolysis, giving not only the ring-opened product of the pyrrolidone moiety of the pGlu residue, but also the cleavage product of the pGlu-peptide linkage. The ring- opening reaction predominated over the cleavage reaction in hydrolysis of the four peptides in 1 N HCl at 60°C. The ring-opening reaction and the cleavage reaction of pGlu-peptide linkage proceeded faster than the cleavage of internal peptide bonds. The rate of hydrolysis was affected by the reaction temperature, and the ring-opening reaction was greatly diminished at 4°C in comparison with the cleavage reaction. Thus, the phenomenon that the pGlu- peptide bond is susceptible to dilute HCl as compared to the other peptide bonds appears to be a general one.
High Performance Liquid Chromatography (HPLC.) of Natural Products. III . Isolation of New Tripeptides from the Fermentation Broth of P. Chrysogenum
Neuss, N.,Miller, R. D.,Affolder, C. A.,Nakatsukasa, W.,Mabe, J.,et al.
, p. 1119 - 1129 (1980)
α-Aminoadipoyl-alanyl-valine, α-aminoadipoyl-serinyl-valine and α-aminoadipoyl-serinyl-isodehydrovaline have been isolated from the fermentation broth of P. chrysogenum.The configuration of α-aminoadipoyl-serinyl-valine has been shown to be L, L, D.
Biphasic One-Pot Synthesis of Two Useful and Separable Compounds Using Cofactor-Requiring Enzymatic Reactions: Glutamate Dehydrogenase Catalyzed Synthesis of L-α-Aminoadipate Coupled with Alcohol Dehydrogenase Catalyzed ASynthesis of a Chiral Lactone
Matos, Jose R.,Wong, Chi-Huey
, p. 2388 - 2389 (1986)
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Studies on acylase activity and micro-organisms. XVII. Optical resolution of tryptophan, 2-aminohexanedioic acid, and 2-aminooctanoic acid by metabolism of soil baceteria on benzoyl derivatives of DL-amino acids.
KAMEDA,MATSUI,KIMURA,TOYOURA,TAKEUCHI
, p. 827 - 830 (1962)
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NEW SYNTHESIS OF L-α-AMINOADIPIC ACID
Belyaev, A. A.,Krasko, E. V.
, p. 1316 (1992)
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Colony-wise Analysis of a Theonella swinhoei Marine Sponge with a Yellow Interior Permitted the Isolation of Theonellamide i
Fukuhara, Kazuya,Takada, Kentaro,Watanabe, Ryuichi,Suzuki, Toshiyuki,Okada, Shigeru,Matsunaga, Shigeki
, p. 2595 - 2599 (2018/12/13)
There are several examples of marine organisms whose metabolic profiles differ among conspecifics inhabiting the same region. We have analyzed the metabolic profile of each colony of a Theonella swinhoei marine sponge with a yellow interior and noticed the patchy distribution of one metabolite. This compound was isolated and its structure was studied by a combination of spectrometric analyses and chemical degradation, showing it to be a congener in the theonellamide class of bicyclic peptides. Theonellamides had previously been isolated by us only from T. swinhoei with a white interior and not from those with a yellow interior.
WA8242A1, A2 and B, novel secretary phospholipase A2 inhibitors produced by Streptomyces violaceusniger. III. Structure elucidation and total synthesis of WA8242B
Yoshimura, Seiji,Otsuka, Takanao,Takase, Shigehiro,Okamoto, Masanori,Okada, Satoshi,Hemmi, Keiji
, p. 655 - 664 (2007/10/03)
The structure of WA8242B, a potent novel inhibitor against phospholipase A2, was fully characterized by spectroscopic methods and chemical degradation. The success of total synthesis of WA8242B confirmed the structure and allowed the pharmacological study of WA8242B. The structures of WA8242A1 and A2 were also described.
