Methyltransferase Contingencies in the Pathway of Everninomicin D Antibiotics and Analogues

Everninomicins are orthoester oligosaccharide antibiotics with potent activity against multidrug-resistant bacterial pathogens. Everninomicins act by disrupting ribosomal assembly in a distinct region in comparison to clinically prescribed drugs. We employed microporous intergeneric conjugation with Escherichia coli to manipulate Micromonospora for targeted gene-replacement studies of multiple putative methyltransferases across the octasaccharide scaffold of everninomicin effecting the A₁, C, F, and H rings. Analyses of gene-replacement and genetic complementation mutants established the mutability of the everninomicin scaffold through the generation of 12 previously unreported analogues and, together with previous results, permitted assignment of the ten methyltransferases required for everninomicin biosynthesis. The in vitro activity of A₁- and H-ring-modifying methyltransferases demonstrated the ability to catalyze late-stage modification of the scaffold on an A₁-ring phenol and H-ring C-4’ hydroxy moiety. Together these results establish the potential of the everninomicin scaffold for modification through mutagenesis and in vitro modification of advanced biosynthetic intermediates.     

海湾战争后防空系统及雷达电子设备的新发展

本文针对海湾战争后的新形势,介绍了战略防御的新构想、战术防空导弹系统及21世纪的防空概念,论述了AEW、AWACS、战场监视目标攻击雷达及其它雷达的最新发展情况,此外,还对国外的反隐身技术进展情况作了介绍。     

Criticality perturbations on inserting small specimens

Translated from Atomnaya Énergiya, Vol. 66, No. 2, pp. 79–81, February, 1989.     

A single mutation Asp229 --> Ser confers upon Gs alpha the ability to interact with regulators of G protein signaling

RGS proteins (regulators of G protein signaling) are GTPase activating proteins (GAPs) for Gi and Gq families of heterotrimeric G proteins but have not been found to interact with Gs alpha. The Gs alpha residue Asp229 has been suggested to be responsible for the inability of RGS proteins to interact with Gs alpha [Natochin, M., and Artemyev, N. O. (1998) J. Biol. Chem. 273, 4300-4303]. To test this hypothesis, we have investigated the possibility of generating an interaction between Gs alpha and RGS proteins by substituting Gs alpha Asp229 with Ser and replacing the potential Gs alpha Asp229 contact residues in RGS16, Glu129 and Asn131, by Ala and Ser, respectively. RGS16 and its mutants failed to interact with Gs alpha. A single mutation of Gs alpha, Asp229Ser, rendered the Gs alpha subunit with the ability to interact with RGS16 and RGS4. Like RGS protein binding to Gi and Gq alpha-subunits, RGS16 preferentially recognized the AlF4--bound conformation of Gs alpha Asp229Ser. In a single-turnover assay, RGS16 maximally stimulated GTPase activity of Gs alpha Asp229Ser by approximately 5-fold with an EC50 value of 7.5 microM. Our findings demonstrate that Asp229 of Gs alpha represents a major barrier for Gs alpha interaction with known RGS proteins.     

非贵金属催化5-羟甲基糠醛选择氧化的研究进展

5-羟甲基糠醛（HMF）作为一种连接生物质资源和精细化学品工业的多功能平台化合物,因含有醛基、羟甲基而具有非常活泼的化学性质。HMF催化选择氧化在生物质转化过程中具有十分重要的意义,近年来受到研究者们的广泛关注。其氧化产物如2,5-呋喃二甲醛（DFF）和2,5-呋喃二甲酸（FDCA）都是具有高附加值的精细化学品,可用于抗菌剂、医药中间体、合成聚酯等方面。非贵金属催化剂因具备低成本、资源丰富以及环境友好的优势,用于HMF选择氧化的相关报道已逐渐增多。阐述了HMF选择氧化的催化反应机理,着重从非贵金属催化剂的角度出发,对近年来HMF的不同催化氧化体系进行了总结和归纳。最后,展望了HMF选择氧化的研究前景,为构建绿色、高效的催化体系提供思路和参考。     

丝素蛋白膜上5-氟尿嘧啶的固定及其释放性能研究

蚕丝丝素膜是弱两性天然高分子荷电膜，用丝素膜作载体，固定抗肿病药5-氟尿嘧喧，并探索其在pH＝3、7、9，25℃下的缓释性能。结果表明：适量的5-氧尿嘧啶能够固定在丝素膜上，且经过丝素涂层保护，5-FU释放速率变慢，释放时间可以延长；在酸性条件下缓释效果好。     

Combustion Regime Monitoring by Flame Imaging and Machine Learning

A method for automatic determination of combustion regimes using flame images on the basis of a convolutional neural network on labeled data is under consideration. It is shown that the accuracy of regime classification reaches 98% on the flame images of a gas burner. The results of the operation of the convolutional neural network and classification using different linear models are compared.