3 +/- 11.6%). MEAM1 longevity and fecundity were highest on tomato (14.7 +/- 1.7 days and 82.4 +/- 9.9 eggs), while AsiaII

1 longevity and fecundity were highest on cotton (23.7 +/- 2.5 days and 135.2 +/- 13.6 eggs). The MEAM1 intrinsic rates of increase (r(m)) on cotton and vegetable were similar (0.08-0.10), whereas the AsiaII 1 r(m) on cotton (0.15) was higher than on vegetables (0.11-0.13). The biology of MEAM1 from Pakistan was compared with published studies; it had a consistently slower rate of development, lower percentage survival, lower adult longevity, longer generation time, lower net reproductive rate and lower r(m). CONCLUSIONS: MEAM1 performed similarly across all hosts, whereas AsiaII 1 performed better on cotton. The comparison between the Pakistani MEAM1 with Sapanisertib published studies suggests that the invasive MEAM1 may have higher performance. (C) 2013 Society of Chemical Industry”
“A newly isolated strain, SJY1, identified as Ochrobactrum sp., utilizes nicotine as a sole source of carbon, nitrogen, and energy. Strain SJY1 could efficiently degrade

VX-680 datasheet nicotine via a variant of the pyridine and pyrrolidine pathways (the VPP pathway), which highlights bacterial metabolic diversity in relation to nicotine degradation. A 97-kbp DNA fragment containing six nicotine degradation-related genes was obtained by gap closing from the genome sequence of strain SJY1. Three genes, designated vppB, vppD, and vppE, in the VPP pathway were cloned and heterologously expressed, and the related proteins were characterized. The vppB gene encodes a flavin-containing amine oxidase converting 6-hydroxynicotine to 6-hydroxy-N-methylmyosmine. Although VppB specifically catalyzes the dehydrogenation of 6-hydroxynicotine rather than nicotine, it shares higher amino acid sequence identity with nicotine oxidase (38%) from the pyrrolidine pathway than with its isoenzyme

(6-hydroxy-L-nicotine oxidase, 24%) from the pyridine pathway. The vppD gene encodes an NADH-dependent flavin-containing monooxygenase, which catalyzes the hydroxylation of 6-hydroxy-3-succinoylpyridine to 2,5-dihydroxypyridine. VppD shows 62% amino acid sequence Kinase Inhibitor Library cell line identity with the hydroxylase (HspB) from Pseudomonas putida strain S16, whereas the specific activity of VppD is similar to 10-fold higher than that of HspB. VppE is responsible for the transformation of 2,5-dihydroxypyridine. Sequence alignment and phylogenetic analysis suggested that the VPP pathway, which evolved independently from nicotinic acid degradation, might have a closer relationship with the pyrrolidine pathway. The proteins and functional pathway identified here provide a sound basis for future studies aimed at a better understanding of molecular principles of nicotine degradation.”
“Anthracene-polyamine conjugates inhibit the in vitro proliferation of the intraerythrocytic human malaria parasite Plasmodium falciparum, with 50% inhibitory concentrations (IC(50)s) in the nM to mu M range.