32466-54-9Relevant articles and documents
Structures and biosynthesis of aflastatins: Novel inhibitors of aflatoxin production by Aspergillus parasiticus
Ono, Makoto,Sakuda, Shohei,Ikeda, Hiroyuki,Furihata, Kazuo,Nakayama, Jiro,Suzuki, Akinori,Isogai, Akira
, p. 1019 - 1028 (1998)
Two novel inhibitors of aflatoxin production by Aspergillus parasiticus were isolated from the mycelial extracts of Streptomyces sp. MRI142 and termed aflastatin A and B. The structures of aflastatin A (1) and B (5) were elucidated by NMR and chemical degradation experiments. These compounds have a novel skeleton of a tetramic acid derivative with a highly oxygenated long alkyl chain. The incorporation experiments using 13C-labeled acetates, propionate, glucose and glycolate suggested that most of the C2 and C3 units involved in the alkyl chain moiety of aflastatin A were biosynthesized from acetic and propionic acids, but five C2 units in the alkyl chain originated from glycolic acid.
Synthesis and evaluation of analogues of the glycinocin family of calcium-dependent antibiotics
Corcilius, Leo,Liu, Dennis Y.,Ochoa, Jessica L.,Linington, Roger G.,Payne, Richard J.
, p. 5310 - 5320 (2018/08/03)
The glycinocins are a class of calcium-dependent, acidic cyclolipopeptide antibiotics that are structurally related to the clinically approved antibiotic daptomycin. In this article, we describe the synthesis of a small library of glycinocin analogues that differ by variation in the exocyclic fatty acyl substituent. The glycinocin analogues were screened against a panel of Gram-positive bacteria (as well as Gram-negative P. aeruginosa). These analogues exhibited similar calcium-dependent activity to the parent natural products against Gram-positive bacteria but showed no activity against P. aeruginosa. The length of the fatty acid was shown to be important for optimal biological activity, while the hybridisation at the α,β position and branching within the fatty acyl chain had only subtle effects on activity.
Synthesis of α,β-unsaturated aldehydes as potential substrates for bacterial luciferases
Brodl, Eveline,Ivkovic, Jakov,Tabib, Chaitanya R.,Breinbauer, Rolf,Macheroux, Peter
, p. 1487 - 1495 (2017/02/18)
Bacterial luciferase catalyzes the monooxygenation of long-chain aldehydes such as tetradecanal to the corresponding acid accompanied by light emission with a maximum at 490?nm. In this study even numbered aldehydes with eight, ten, twelve and fourteen carbon atoms were compared with analogs having a double bond at the α,β-position. These α,β-unsaturated aldehydes were synthesized in three steps and were examined as potential substrates in vitro. The luciferase of Photobacterium leiognathi was found to convert these analogs and showed a reduced but significant bioluminescence activity compared to tetradecanal. This study showed the trend that aldehydes, both saturated and unsaturated, with longer chain lengths had higher activity in terms of bioluminescence than shorter chain lengths. The maximal light intensity of (E)-tetradec-2-enal was approximately half with luciferase of P. leiognathi, compared to tetradecanal. Luciferases of Vibrio harveyi and Aliivibrio fisheri accepted these newly synthesized substrates but light emission dropped drastically compared to saturated aldehydes. The onset and the decay rate of bioluminescence were much slower, when using unsaturated substrates, indicating a kinetic effect. As a result the duration of the light emission is doubled. These results suggest that the substrate scope of bacterial luciferases is broader than previously reported.
