Сравнительный протеомный и транскриптомный анализ устойчивого к нитрон-олигомицину мутантного штамма Streptomyces fradiae -nitR + bld

2020 ◽  
Vol 56 (9) ◽  
pp. 1098-1102
Author(s):  
О. Б. Беккер ◽  
А. А. Ватлин ◽  
Д. А. Мавлетова ◽  
Л. Н. Лысенкова ◽  
А. Е. Щекотихин ◽  
...  
Keyword(s):  
Streptomyces Fradiae

Comparative Proteomic and Transcriptome Analysis of Nitron-Oligomycin Resistant Mutant Streptomyces fradiae-nitR+bld Strain

2020 ◽  
Vol 56 (9) ◽  
pp. 1151-1154
Author(s):  
O. B. Bekker ◽  
A. A. Vatlin ◽  
D. A. Mavletova ◽  
L. N. Lysenkova ◽  
A. E. Shchekotikhin ◽  
...  
Keyword(s):  
Transcriptome Analysis ◽  
Resistant Mutant ◽  
Streptomyces Fradiae

scholarly journals Tetracycline removal from model aqueous solutions by pretreated waste Streptomyces fradiae biomass

2021 ◽  
Vol 35 (1) ◽  
pp. 953-963
Author(s):  
Gergana Kirova ◽  
Zdravka Velkova ◽  
Margarita Stoytcheva ◽  
Velizar Gochev
Keyword(s):  
Aqueous Solutions ◽  
Streptomyces Fradiae

scholarly journals Change in colony morphology and kinetics of tylosin production after UV and gamma irradiation mutagenesis of Streptomyces fradiae NRRL-2702

2009 ◽  
Vol 164 (4) ◽  
pp. 469-477 ◽  
Author(s):  
Shazia Khaliq ◽  
Kalsoom Akhtar ◽  
Muhammad Afzal Ghauri ◽  
Ruqia Iqbal ◽  
Ahmad Mukhtar Khalid ◽  
...  
Keyword(s):  
Gamma Irradiation ◽  
Colony Morphology ◽  
Streptomyces Fradiae ◽  
Kinetics Of

scholarly journals Elucidation of structure of novel macrolide antibiotics produced by mutant strains of Streptomyces fradiae.

1983 ◽  
Vol 36 (4) ◽  
pp. 376-382 ◽  
Author(s):  
H. A. KIRST ◽  
G. M. WILD ◽  
R. H. BALTZ ◽  
E. T. SENO ◽  
R. L. HAMILL ◽  
...  
Keyword(s):  
Macrolide Antibiotics ◽  
Streptomyces Fradiae ◽  
Mutant Strains

Properties of NAD-dependent glutamate dehydrogenase from the tylosin producer Streptomyces fradiae

1997 ◽  
Vol 43 (11) ◽  
pp. 1005-1010 ◽  
Author(s):  
Kien Trung Nguyen ◽  
Lieu Thi Nguyen ◽  
Jan Kopecký ◽  
Vladislav Běhal
Keyword(s):  
Key Words ◽  
Glutamate Dehydrogenase ◽  
Reductive Amination ◽  
Divalent Cations ◽  
Ammonium Assimilation ◽  
Alkaline Ph ◽  
Streptomyces Fradiae ◽  
Oxidative Deamination

Glutamate dehydrogenase is an enzyme responsible for ammonium assimilation and glutamate catabolism in organisms. The tylosin producer Streptomyces fradiae possesses both NADP- and NAD-dependent glutamate dehydrogenases. The latter enzyme was purified 498-fold with a 7.5% recovery by a six-step protocol. The enzyme is composed of two subunits, each of Mr 47 000, and could form active aggregates of four or eight subunits. Its activity was inactivated by alkaline pH or temperatures of −20 °C or above 40 °C. Activities assayed in the direction of oxidative deamination and reductive amination were optimal at pH 9.2 and 8.8, respectively, and at temperatures of 30–35 °C. No activity was found when NAD(H) was replaced with NADP(H). The Km values were 32.2 mM for L-glutamate, 0.3 mM for NAD+, 3.4 mM for 2-ketoglutarate, 14.2 mM for NH4+, and 0.05 mM for NADH. Deamination activity was partially inhibited by adenyl nucleotides and several divalent cations; amination activity was not affected by the nucleotides but significantly inhibited by Cu2+ or Ni2+.Key words: Streptomyces fradiae, NAD-dependent glutamate dehydrogenase, purification, properties.

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