Nomenclature Abstract for Streptomyces noursei Brown et al. 1953 (Approved Lists 1980) emend. Nouioui et al. 2018.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
George M Garrity
Keyword(s):  
Streptomyces Noursei

ATP levels in phosphate-deregulated and arsenate-resistant mutants of Streptomyces noursei

1984 ◽  
Vol 24 (4) ◽  
pp. 239-245
Author(s):  
F. Hänel ◽  
U. Gräfe ◽  
W. Friedrich ◽  
E. J. Bormann
Keyword(s):  
Atp Levels ◽  
Streptomyces Noursei ◽  
Resistant Mutants

A novel antibiotic produced by streptomyces noursei Da07210

2009 ◽  
Vol 96 (1) ◽  
pp. 109-112 ◽  
Author(s):  
Xiaopeng Wu ◽  
Huiqin Huang ◽  
Guangying Chen ◽  
Qianguang Sun ◽  
Jie Peng ◽  
...  
Keyword(s):  
Streptomyces Noursei

Alcohol-induced switching over of metabolic flux in Streptomyces noursei JA0 3890b

1979 ◽  
Vol 19 (10) ◽  
pp. 721-726
Author(s):  
U. Gräfe ◽  
W. Schade ◽  
H. Bocker ◽  
H. Thrum
Keyword(s):  
Metabolic Flux ◽  
Streptomyces Noursei

scholarly journals Initiation of Polyene Macrolide Biosynthesis: Interplay between Polyketide Synthase Domains and Modules as Revealed via Domain Swapping, Mutagenesis, and Heterologous Complementation

2011 ◽  
Vol 77 (19) ◽  
pp. 6982-6990 ◽  
Author(s):  
Sondre Heia ◽  
Sven E. F. Borgos ◽  
Håvard Sletta ◽  
Leticia Escudero ◽  
Elena M. Seco ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Fungal Infections ◽  
Domain Swapping ◽  
Site Directed Mutagenesis ◽  
Active Site Residue ◽  
Polyene Macrolide ◽  
Content Type ◽  
Streptomyces Noursei ◽  
Strict Specificity ◽  
Different Levels

ABSTRACTPolyene macrolides are important antibiotics used to treat fungal infections in humans. In this work, acyltransferase (AT) domain swaps, mutagenesis, and cross-complementation with heterologous polyketide synthase domain (PKS) loading modules were performed in order to facilitate production of new analogues of the polyene macrolide nystatin. Replacement of AT0in the nystatin PKS loading module NysA with the propionate-specific AT1from the nystatin PKS NysB, construction of hybrids between NysA and the loading module of rimocidin PKS RimA, and stepwise exchange of specific amino acids in the AT0domain by site-directed mutagenesis were accomplished. However, none of the NysA mutants constructed was able to initiate production of new nystatin analogues. Nevertheless, many NysA mutants and hybrids were functional, providing for different levels of nystatin biosynthesis. An interplay between certain residues in AT0and an active site residue in the ketosynthase (KS)-like domain of NysA in initiation of nystatin biosynthesis was revealed. Some hybrids between the NysA and RimA loading modules carrying the NysA AT0domain were able to prime rimocidin PKS with both acetate and butyrate units upon complementation of arimA-deficient mutant of the rimocidin/CE-108 producerStreptomyces diastaticus. Expression of the PimS0 loading module from the pimaricin producer in the same host, however, resulted in production of CE-108 only. Taken together, these data indicate relaxed substrate specificity of NysA AT0domain, which is counteracted by a strict specificity of the first extender module KS domain in the nystatin PKS ofStreptomyces noursei.

scholarly journals PRODUCTION OF NITRAMINOACETIC ACID BY STREPTOMYCES NOURSEI 8054-MC3

1968 ◽  
Vol 21 (4) ◽  
pp. 279-282 ◽  
Author(s):  
YUKIO MIYAZAKI ◽  
YOSHIKI KONO ◽  
AKIRA SHIMAZU ◽  
SETSUO TAKEUCHI ◽  
HIROSHI YONEHARA
Keyword(s):  
Streptomyces Noursei

scholarly journals Mutual relation of three pock-forming plasmids resident in Streptomyces noursei.

1985 ◽  
Vol 38 (3) ◽  
pp. 390-400 ◽  
Author(s):  
IKUO KOJIMA ◽  
TOMOKO NANJYO ◽  
MASANORI OKANISHI
Keyword(s):  
Mutual Relation ◽  
Streptomyces Noursei

Scale-up and scale-down techniques for fermentations of polyene antibiotics

1990 ◽  
Vol 55 (7) ◽  
pp. 1730-1740 ◽  
Author(s):  
Petr Ettler
Keyword(s):  
Dehydrogenase Activity ◽  
Scale Up ◽  
Scaling Up ◽  
Industrial Scale ◽  
Laboratory Findings ◽  
Polyene Antibiotics ◽  
Activity Determination ◽  
Simultaneous Control ◽  
Streptomyces Noursei ◽  
Scale Down

Our philosophy of successful biotechnology transfer to industrial scale covers the comparison of complex sets of microbiological, analytical and bioengineering data from cultivations in various scales and different geometries of mixing with laboratory findings. In particular, the availability of nutrients to producing microorganism should be understood, therefore for quick scaling-up procedure of polyene antibiotics produced by Streptomyces noursei we recommend to use physiological marker as total dehydrogenase activity determination. The utility of scale-down tests for identification of process fluctuation, validation of new substrate batches and simultaneous control of inoculum quality was proved.

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