
We thank Fermentek for the information, the free Nonactin granted for our project, and most of all, the moral support |
Link friends 17dmag 7aad actinomycin alfatoxin-b1 aflatoxin-b2 aflatoxin-g1 aflatoxin-g2 aflatoxin-m1 aflatoxin-m2 anisomycin ascomycin Blukher Bukharin dybenko frinovsky geldanamycin k252a k252b kt5720 kt5823 leptomycin Link-Exchange mithramycin mitomycin nonactin Ochratoxin parthenolide Snorring staurosporine tinnitus trichostatin tukhachevsky verruculogen vomitoxin wortmannin yakir yegorov yezhov zearalenone
Here come some links to top-rated hrefs, such as Microsoft, wikipedia, Google and Yahoo :google, microsoft, yahoo, wikipedia
Now come links to these of fermentek product pages, that are needy : .the homepage of fermentek, FK506 or tacrolimus, products of Fermentek: staurosporine, K252A, aflatoxin, Sirolimus (Rapamycin) And other link beggars: Tinnitus. about some guys that had tinnitus | Antimicrob Agents Chemother. 1999 Jul;43(7):1662-8. Nonactin biosynthesis: the product of nonS catalyzes the formation of the furan ring of nonactic acid.
Woo AJ, Strohl WR, Priestley ND.
Department of Microbiology, The Ohio State University, Columbus, Ohio 43210, USA.
Nonactin is the parent compound of a group of ionophore antibiotics, known as the macrotetrolides, produced by Streptomyces griseus subsp. griseus ETH A7796. Nonactin is a significant compound because of its inhibitory effects on the P170 glycoprotein-mediated efflux of chemotherapeutic agents in multiple-drug-resistant cancer cells. Nonactin is also significant in that it is a highly atypical polyketide. Very little is presently known about the genes of the nonactin biosynthesis cluster. In this paper we describe our efforts to establish a connection between the product of a gene from the nonactin biosynthesis cluster and a known biochemical transformation in nonactin biosynthesis. Nonactate synthase is the enzyme which catalyzes the formation of nonactic acid from an acyclic precursor in nonactin biosynthesis. We have synthesized the substrate for this enzyme and have detected the in vitro cyclization activity of the substrate in cell-free preparations of S. griseus subsp. griseus ETH A7796. Previous studies by R. Plater and J. A. Robinson (Gene 112:117-122, 1992) had suggested, based on sequence homology, that the product of a partial open reading frame found close to the tetranactin resistance gene of S. griseus could be the nonactate synthase. We have therefore cloned, sequenced, and heterologously expressed this full gene (nonS), and we have shown that the gene product, NonS, does indeed catalyze the formation of the furan ring of nonactic acid as hypothesized.
PMID: 10390219 |
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