1783-96-6Relevant articles and documents
Harada
, p. 590 (1965)
Structure, mechanism, and substrate profile for Sco3058: The closest bacterial homologue to human renal dipeptidase
Cummings, Jennifer A.,Nguyen, Tinh T.,Fedorov, Alexander A.,Kolb, Peter,Xu, Chengfu,Fedorov, Elena V.,Shoichet, Brian K.,Barondeau, David P.,Almo, Steven C.,Raushel, Frank M.
, p. 611 - 622 (2010)
Human renal dipeptidase, an enzyme associated with glutathione metabolism and the hydrolysis of β-lactams, is similar in sequence to a cluster of ～400 microbial proteins currently annotated as nonspecific dipeptidases within the amidohydrolase superfamily. The closest homologue to the human renal dipeptidase from a fully sequenced microbe is Sco3058 from Streptomyces coelicolor. Dipeptide substrates of Sco3058 were identified by screening a comprehensive series of L-Xaa-L-Xaa, L-Xaa-D-Xaa, and D-Xaa-L-Xaa dipeptide libraries. The substrate specificity profile shows that Sco3058 hydrolyzes a broad range of dipeptides with a marked preference for an L-amino acid at the N-terminus and a D-amino acid at the C-terminus. The best substrate identified was L-Arg-D-Asp (kcat/Km = 7.6 x 105 M -1 s-1). The three-dimensional structure of Sco3058 was determined in the absence and presence of the inhibitors citrate and a phosphinate mimic of L-Ala-D-Asp. The enzyme folds as a (β/α)8 barrel, and two zinc ions are bound in the active site. Site-directed mutagenesis was used to probe the importance of specific residues that have direct interactions with the substrate analogues in the active site (Asp-22, His-150, Arg-223, and Asp-320). The solvent viscosity and kinetic effects of D2O indicate that substrate binding is relatively sticky and that proton transfers do not occurr during the rate-limiting step. A bell-shaped pH-rate profile for kcat and kcat/Km indicated that one group needs to be deprotonated and a second group must be protonated for optimal turnover. Computational docking of high-energy intermediate forms of L/D-Ala-L/D-Ala to the three-dimensional structure of Sco3058 identified the structural determinants for the stereochemical preferences for substrate binding and turnover.
Propagation of biochirality: Crossovers and nonclassical crystallization kinetics of aspartic acid in water
Lee, Tu,Lin, Yu Kun,Tsai, Ya Chung,Lee, Hung Lin
, p. 768 - 779 (2013)
All experimental procedures discussed could be treated as a screening tool for probing the existence of molecular association among the chiral molecules and the solvent system. The molecular association phases of a racemic conglomerate solution (CS) and a
Structural and functional analysis of pantocin A: An antibiotic from Pantoea agglomerans discovered by heterologous expression of cloned genes
Jin, Mi,Liu, Liang,Wright, Sandra A. I.,Beer, Steven V.,Clardy, Jon
, p. 2898 - 2901 (2003)
Small-molecule chemistry and biochemical techniques have been used to determine the structure and mode of function of pantocin A (see structure), a naturally occurring antibiotic. Pantocin A functions as an inhibitor of histidine biosynthesis, as shown by its ability to inhibit the action of L-histidinol phosphate aminotransferase, which converts imidazole acetol phosphate to L-histidinol phosphate in Escherichia coli.
Optical Resolution of Aspartic Acid by Using Copper Complexes of Optically Active Amino Acids
Harada, Kaoru,Fujii, Noriko
, p. 653 - 654 (1983)
DL-Aspartic acid was resolved with high optical purity in the presence of an optically active amino acid copper complex.The mechanism of the optical resolution was explained by the competitive inhibition of crystallization.
Racemization of the aspartic acid residue of amyloid-β peptide by a radical reaction
Tambo, Koharu,Yamaguchi, Tomomi,Kobayashi, Keiko,Terauchi, Eri,Ichi, Ikuyo,Kojo, Shosuke
, p. 416 - 418 (2013)
Human amyloid-β peptide 1-42 (Aβ) was subjected to a radical reaction by using ascorbic acid and CuCl2. The percentage of D-aspartic acid (D-Asp) after 24 h had increased to 6.69 ± 0.09%, this being comparable with the reported D-Asp concentration of purified core amyloids in Alzheimer's disease patients. This racemization was significantly inhibited by radical scavengers. L-Alanine was also racemized during the same reaction.
Switchable Chiral Selection of Aspartic Acids by Dynamic States of Brushite
Jiang, Wenge,Pan, Haihua,Zhang, Zhisen,Qiu, S. Roger,Kim, J. Dongun,Xu, Xurong,Tang, Ruikang
, p. 8562 - 8569 (2017)
We herein show the chiral recognition and separation of aspartic acid (Asp) enantiomers by achiral brushite due to the asymmetries of their dynamical steps in its nonequilibrium states. Growing brushite has a higher adsorption affinity to d-Asp, while l-A
Harada
, p. 1552,1554 (1965)
Noncovalently Functionalized Commodity Polymers as Tailor-Made Additives for Stereoselective Crystallization
Wan, Xinhua,Wang, Zhaoxu,Ye, Xichong,Zhang, Jie
supporting information, p. 20243 - 20248 (2021/08/09)
Stereoselective inhibition of the nucleation and crystal growth of one enantiomer aided by “tailor-made” polymeric additives is an efficient method to obtain enantiopure compounds. However, the conventional preparation of polymeric additives from chiral monomers are laborious and limited in structures, which impedes their rapid optimization and applicability. Herein, we report a “plug-and-play” strategy to facilitate synthesis by using commercially available achiral polymers as the platform to attach various chiral small molecules as the recognition side-chains through non-covalent interactions. A library of supramolecular polymers made up of two vinyl polymers and six small molecules were applied with seeds in the selective crystallization of seven racemates in different solvents. They showed good to excellent stereoselectivity in yielding crystals with high enantiomeric purities in conglomerates and racemic compound forming systems. This convenient, low-cost modular synthesis strategy of polymeric additives will allow for high-efficient, economical resolution of various racemates on different scales.
Unique polyhalogenated peptides from the marine sponge Ircinia sp.
Fernández, Rogelio,Bayu, Asep,Hadi, Tri Aryono,Bueno, Santiago,Pérez, Marta,Cuevas, Carmen,Putra, Masteria Yunovilsa
, (2020/08/28)
Two new bromopyrrole peptides, haloirciniamide A (1) and seribunamide A (2), have been isolated from an Indonesian marine sponge of the genus Ircinia collected in the Thousand Islands (Indonesia). The planar structure of both compounds was assigned on the basis of extensive 1D and 2D NMR spectroscopy and mass spectrometry. The absolute configuration of the amino acid residues in 1 and 2 was determined by the application of Marfey's method. Compound 1 is the first dibromopyrrole cyclopeptide having a chlorohistidine ring, while compound 2 is a rare peptide possessing a tribromopyrrole ring. Both compounds failed to show significant cytotoxicity against four human tumor cell lines, and neither compound was able to inhibit the enzyme topoisomerase I or impair the interaction between programmed cell death protein PD1 and its ligand, PDL1.
Covalent Organic Frameworks with Chirality Enriched by Biomolecules for Efficient Chiral Separation
Zhang, Sainan,Zheng, Yunlong,An, Hongde,Aguila, Briana,Yang, Cheng-Xiong,Dong, Yueyue,Xie, Wei,Cheng, Peng,Zhang, Zhenjie,Chen, Yao,Ma, Shengqian
supporting information, p. 16754 - 16759 (2018/11/27)
The separation of racemic compounds is important in many fields, such as pharmacology and biology. Taking advantage of the intrinsically strong chiral environment and specific interactions featured by biomolecules, here we contribute a general strategy is developed to enrich chirality into covalent organic frameworks (COFs) by covalently immobilizing a series of biomolecules (amino acids, peptides, enzymes) into achiral COFs. Inheriting the strong chirality and specific interactions from the immobilized biomolecules, the afforded biomolecules?COFs serve as versatile and highly efficient chiral stationary phases towards various racemates in both normal and reverse phase of high-performance liquid chromatography (HPLC). The different interactions between enzyme secondary structure and racemates were revealed by surface-enhanced Raman scattering studies, accounting for the observed chiral separation capacity of enzymes?COFs.
