[Roles of geldanamycin biosynthetic genes in Streptomyces hygroscopicus 17997]. 2008

Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences & Peking Union Medical College, Key Laboratory of Biotechnology of Antibiotics of Ministry of Health, Beijing 100050, China.

Geldanamycin (Gdm), an inhibitor of heat shock protein 90 (Hsp90), shows antitumor and antivirus bioactivity. Most Geldanamycin biosynthetic genes have been cloned from the genome library of Streptomyces hygroscopicus 17997. In this report, polyketide synthase (pks) gene, mono-oxygenase (gdmM) gene and carbamoyltransferase gene (gdmN) were subjected to inactivation. Three gene disrupted mutants (deltapks, deltagdmM and deltagdmN) were obtained by double crossover. No Geldanamycin production was detected in three mutant strains cultured in fermentation broth. Gene complementation experiments excluded the possible polar effect of gene disruption on other genes. These results confirmed that pks, gdmM and gdmN genes were essential for Geldanamycin biosynthesis.

UI MeSH Term Description Entries
D006899 Mixed Function Oxygenases Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation. Hydroxylase,Hydroxylases,Mixed Function Oxidase,Mixed Function Oxygenase,Monooxygenase,Monooxygenases,Mixed Function Oxidases,Function Oxidase, Mixed,Function Oxygenase, Mixed,Oxidase, Mixed Function,Oxidases, Mixed Function,Oxygenase, Mixed Function,Oxygenases, Mixed Function
D013302 Streptomyces A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.
D016227 Benzoquinones Benzene rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups. 1,2-Benzoquinones,1,4-Benzoquinones,Benzodiones,2,5-Cyclohexadiene-1,4-Diones,o-Benzoquinones,p-Benzoquinones
D047029 Lactams, Macrocyclic LACTAM-forming compounds with a ring size of approximately 1-3 dozen atoms. Ansamycins,Macrocyclic Lactams
D048630 Polyketide Synthases Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides. Polyketide Synthase,6-Deoxyerythronolide-B Synthase,Epothilone Polyketide Synthase,Erythromycin Polyketide Synthase,Griseusin Polyketide Synthase,Niddamycin Polyketide Synthase,Polyketide Synthase L1,Polyketide Synthase WA,Rifamycin Polyketide Synthase,Sterigmatocystin Polyketide Synthase,Type I Polyketide Synthase,Type II Polyketide Beta-Ketoacyl Synthase,Urdamycin Polyketide Synthase,WdPKS1 Protein,WhiE Polyketide Synthase,6 Deoxyerythronolide B Synthase,Polyketide Synthase, Epothilone,Polyketide Synthase, Erythromycin,Polyketide Synthase, Griseusin,Polyketide Synthase, Niddamycin,Polyketide Synthase, Rifamycin,Polyketide Synthase, Sterigmatocystin,Polyketide Synthase, Urdamycin,Polyketide Synthase, WhiE,Protein, WdPKS1,Synthase L1, Polyketide,Synthase WA, Polyketide,Synthase, 6-Deoxyerythronolide-B,Synthase, Epothilone Polyketide,Synthase, Erythromycin Polyketide,Synthase, Griseusin Polyketide,Synthase, Niddamycin Polyketide,Synthase, Polyketide,Synthase, Rifamycin Polyketide,Synthase, Sterigmatocystin Polyketide,Synthase, Urdamycin Polyketide,Synthase, WhiE Polyketide,Synthases, Polyketide,Type II Polyketide Beta Ketoacyl Synthase
D019878 Carboxyl and Carbamoyl Transferases A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3. Carbamoyl Transferase,Carbamoyltransferase,Carboxyl Transferase,Carboxyl and Carbamoyl Transferase,Carboxyltransferase,Carbamoyl Transferases,Carbamoyltransferases,Carboxyl Transferases,Carboxyltransferases,Transferase, Carbamoyl,Transferase, Carboxyl,Transferases, Carbamoyl,Transferases, Carboxyl

Related Publications

Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
March 2006, Current microbiology,
Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
November 2006, Sheng wu gong cheng xue bao = Chinese journal of biotechnology,
Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
June 2013, Genetics and molecular research : GMR,
Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
June 2011, Journal of microbiology and biotechnology,
Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
July 2011, Sheng wu gong cheng xue bao = Chinese journal of biotechnology,
Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
May 2013, Journal of natural products,
Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
July 2003, Sheng wu gong cheng xue bao = Chinese journal of biotechnology,
Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
November 2012, Journal of microbiology and biotechnology,
Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
March 2010, Molecules (Basel, Switzerland),
Weiqing He, and Yuying Liu, and Guizhi Sun, and Yiguang Wang
June 2008, Journal of microbiology and biotechnology,
Copied contents to your clipboard!