ライフサイエンスコーパス: Pseudomonas stutzeri

1 lipoferum) and denitrifying bacteria (i.e., Pseudomonas stutzeri).

2 ratory chains, and the gamma-proteobacterium Pseudomonas stutzeri.

3 y oxidized nitric oxide reductase (NOR) from Pseudomonas stutzeri.

4 ration (N = 20) showed a higher abundance of Pseudomonas stutzeri (2.1% versus 1.0%, p = 0.024) and P

5 Nitrous oxide reductase (N(2)OR) from Pseudomonas stutzeri, a dimeric enzyme with a canonical

6 aminoacid was carried out with a lipase from Pseudomonas stutzeri and a protease from Bacillus subtil

7 5, the transfer of an inducible cluster from Pseudomonas stutzeri and Azotobacter vinelandii yields a

8 H NMR spectra of the CuA center of N2OR from Pseudomonas stutzeri, and a mutant enzyme that contains

9 depolymerization of a native EPS produced by Pseudomonas stutzeri AS22.

10 igands for the CuA centre of the enzyme from Pseudomonas stutzeri ATCC14405 were substituted by evolu

11 ulations with a mix of Bacillus subtilis and Pseudomonas stutzeri, bacteria species isolated from the

12 Phosphite dehydrogenase (PTDH) from Pseudomonas stutzeri catalyzes the nicotinamide adenine

13 osphodiesterases, GlpQI and GlpQII, found in Pseudomonas stutzeri DSM4166 and Pseudomonas fluorescens

14 (BIRD-1), Pseudomonas fluorescens SBW25 and Pseudomonas stutzeri DSM4166 was performed in unison wit

15 Enterococcus xiangfangensis (GFB-1), Pseudomonas stutzeri (GFB-2), Bacillus subtilis (GFB-3),

16 der the optimal conditions it was found that Pseudomonas stutzeri lipase and Chromobacterium viscosum

17 In the Cu(A) site of Pseudomonas stutzeri N(2)OR, a histidine ligand was foun

18 eport cryo-electron microscopy structures of Pseudomonas stutzeri NosDFY and its complexes with NosL

19 HBSS bottle and from pericardial tissue grew Pseudomonas stutzeri of the same genotype; however, no P

20 Here we report that the wastewater bacterium Pseudomonas stutzeri OX1 degrades aerobically 0.56 micro

21 t toluene/o-xylene monooxygenase (ToMO) from Pseudomonas stutzeri OX1 is capable of oxidizing arenes,

22 us (Bath), toluene monooxygenase (ToMO) from Pseudomonas stutzeri OX1, and phenol hydroxylase (PH) fr

23 us (Bath), toluene monooxygenase (ToMO) from Pseudomonas stutzeri OX1, and phenol hydroxylase (PH) fr

24 utzeri OX1, and phenol hydroxylase (PH) from Pseudomonas stutzeri OX1.

25 utzeri OX1, and phenol hydroxylase (PH) from Pseudomonas stutzeri OX1.

26 n adaptation to oxygen-limited conditions in Pseudomonas stutzeri (P. stutzeri), a model for the clin

27 Genes important for growth of Pseudomonas stutzeri PDA on chlorate were identified usi

28 o particular residues, Glu175 and Ala176, in Pseudomonas stutzeri phosphite dehydrogenase (PTDH) as t

29 ne dithiocarboxylic acid siderophore, in the Pseudomonas stutzeri proteome.

30 on of streaked Shewanella oneidensis MR1 and Pseudomonas stutzeri RCH2 colonies and further resolve c

31 ) from a metal tolerant groundwater isolate, Pseudomonas stutzeri RCH2 to assess the impact of host-d

32 quencing of an 8182-bp chromosomal region in Pseudomonas stutzeri revealed the major portion of an ap

33 The ability of Pseudomonas stutzeri strain DCP-Ps1 to drive CaCO3 biomi

34 (SMX) contamination, and a laboratory-grown Pseudomonas stutzeri strain, were exposed to 240-520 mug

35 We address this question using consortia of Pseudomonas stutzeri strains, where one is an antibiotic

36 encoding for bacterial cytochrome c-551 from Pseudomonas stutzeri substrain ZoBell has been mutated t

37 red harboring the gene cluster nirFDLGH from Pseudomonas stutzeri substrain ZoBell on a high copy pla

38 he gene nirM, coding for cytochrome c-551 in Pseudomonas stutzeri substrain ZoBell, was engineered to

39 ors diazotrophic (N(2)-fixing) endobacteria (Pseudomonas stutzeri) that allow JGTA-S1 to fix N(2) and

40 TCA16, Pseudomonas putida TCA23 and N7, and Pseudomonas stutzeri TRA27a were able to produce branche

41 Pseudomonas stutzeri was predominantly identified in six

42 Surprisingly, lipase from Pseudomonas stutzeri was the fastest biocatalyst among a

43 The htx and ptx operons of Pseudomonas stutzeri WM88 allow for the use of the inorg

44 The ptxD gene from Pseudomonas stutzeri WM88 encoding the novel phosphorus

45 nalysis of two distinct C-P lyase operons in Pseudomonas stutzeri WM88 were completed.

46 The ptxD gene, derived from Pseudomonas stutzeri WM88, that confers to cells the abi

47 The pathway was identified in Pseudomonas stutzeri WM88, which was chosen for detailed

48 quired for the oxidation of hypophosphite in Pseudomonas stutzeri WM88.

49 osomal RNA operon from the marine bacterium, Pseudomonas stutzeri Zobell, was cloned and characterize

50 shown that, in the oxidized state, heme c of Pseudomonas stutzeri (ZoBell strain) cytochrome cd1 has