منابع مشابه
New bisbenzylisoquinoline alkaloid from Laureliopsis philippiana.
Phytochemical investigation of Laureliopsis philippiana resulted in isolation of a new bisbenzylisoquinoline alkaloid (1) named laureliopsine A. The structure was established by spectroscopic methods, including 2D homo- and heteronuclear NMR experiments. This finding of a bisbenzylisoquinoline alkaloid in Laureliopsis supports its close relationship to Atherosperma and its taxonomic segregation...
متن کاملChapter 771 Actinomadura R39 d-Ala d Ala Carboxypeptidase
bacterial penicillin-binding proteins and beta-lactamases. Antimicrob. Agents Chemother. 42(1), 1 17. [41] Davies, C., White, S.W., Nicholas, R.A. (2001). Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-Å resolution. J. Biol. Chem. 276(1), 616 623. [42] Nicola, G., Tomberg, J., Pratt, R.F., Nicholas, R.A., Davies, C. (2010). Crystal structures of coval...
متن کاملMutational analysis of active-site residues of the enterococcal D-ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-ala-D-Ala ligase and D-ala-D-Ala carboxypeptidase VanY.
BACKGROUND Vancomycin-resistant enterococci are pathogenic bacteria that attenuate antibiotic sensitivity by producing peptidoglycan precursors that terminate in D-Ala-D-lactate rather than D-Ala-D-Ala. A key enzyme in effecting antibiotic resistance is the metallodipeptidase VanX, which reduces the cellular pool of the D-Ala-D-Ala dipeptide. RESULTS We constructed eleven mutants, using the r...
متن کاملBoc-AzAla-Ala-OMe
THE TITLE COMPOUND (SYSTEMATIC NAME tert-butyl 3-{[1-(methoxy-carbon-yl)eth-yl]amino-carbon-yl}-3-methyl-carbazate), C(11)H(21)N(3)O(5), is a precursor for the study of a new class of foldamer based on aza/α-dipeptide oligomerization [Abbas et al. (2009 ▶). Tetra-hedron Lett.50, 4158-4160]. The asymmetric unit consists of one mol-ecule in an extended conformation which is stabilized by inter-mo...
متن کاملInhibition of proteinase K by methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone. An x-ray study at 2.2-A resolution.
The crystal structure of the transition state analog complex formed covalently between proteinase K and methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone was determined by x-ray diffraction methods at a resolution of 2.2 A and refined by constrained least squares to an R factor of 19.8% for the 11864 structure amplitudes greater than 1 sigma F. The chloromethyl ketone group is covalently link...
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ژورنال
عنوان ژورنال: TYCHE – Contributions to Ancient History, Papyrology and Epigraphy
سال: 1993
ISSN: 1010-9161,2409-5540
DOI: 10.15661/tyche.1992.007.26