Die Bildung hydroxylierter Phenazine durch Pseudomonas fluorescens Y4 bei Be2+-Zusatz zum Kulturmedium – ein Abwehrmechanismus? [1] / The Form ation of Hydroxylated Phenazines by Pseudomonas fluorescens Y4 upon Addition of Be2+ to the Culture Medium – a Defense Mechanism?

1991 ◽  
Vol 46 (3-4) ◽  
pp. 194-196 ◽  
Author(s):  
K. Taraz ◽  
E. M. Schaffner ◽  
H. Budzikiewicz ◽  
H. Korth ◽  
G. Pulverer
Keyword(s):  
Carboxylic Acid ◽  
Pseudomonas Fluorescens ◽  
Culture Medium ◽  
Defense Mechanism ◽  
Iron Deficient ◽  
Deficient Medium

Pseudomonas fluorescens Y4 grown in an iron deficient medium produces increased amounts of 2,9-di- and 2,3,9-trihydroxyphenazine-1-carboxylic acid when Be2+ is added to the culture. The significance of the formation of these compounds is discussed.

2,3,9-Trihydroxyphenazin-l-carbonsäure – ein unter Berylliumeinwirkung gebildetes neues Phenazinderivat aus Pseudomonas fluorescens [1] / 2,3,9-Trihydroxyphenazine- l -carboxylic Acid — a New Phenazine Derivative from Pseudomonas fluorescens Grown under Beryllium Stress [1]

1990 ◽  
Vol 45 (4) ◽  
pp. 552-556 ◽  
Author(s):  
K. Taraz ◽  
E. M. Schaffner ◽  
H. Budzikiewicz ◽  
H. Korth ◽  
G. Pulverer
Keyword(s):  
Carboxylic Acid ◽  
Iron Deficiency ◽  
Dicarboxylic Acid ◽  
Pseudomonas Fluorescens ◽  
Structure Elucidation ◽  
Culture Medium ◽  
Phenazine Derivative

In addition to phenazine, phenazine-1-carboxylic acid, phenazine-1,6-dicarboxylic acid and 2,9-dihydroxyphenazine-1-carboxylic acid a new compound, viz. 2,3,9-trihydroxyphenazine-1-carboxylic acid could be isolated from the culture medium of Pseudomonas fluorescens grown under iron deficiency with beryllium added to the culture medium. Its structure elucidation is described.

New Pyoverdin-Type Siderophores from Pseudomonas fluorescens

1990 ◽  
Vol 45 (10) ◽  
pp. 1437-1450 ◽  
Author(s):  
G. Mohn ◽  
K. Taraz ◽  
H. Budzikiewicz
Keyword(s):  
Carboxylic Acid ◽  
Pseudomonas Fluorescens ◽  
Carboxy Group ◽  
Culture Medium ◽  
Spectroscopic Methods ◽  
Amino Group ◽  
N Terminus ◽  
Short Hand ◽  
Degradation Studies

The structures of two new pyoverdins (GM-I and GM-II) isolated from the culture medium of Pseudomonas fluorescens have been elucidated by spectroscopic methods and degradation studies. The pyoverdins consist of a chromophore which could be identified as (1 S)-5-amino-2,3-dihydro-8,9-dihydroxy-1 H-pyrimido[1,2-a]quinoline-1-carboxylic acid substituted at the amino group with a 3-carboxypropanoyl or a succinamoyl residue and at the carboxy group with the N-terminus of D-Ala-D-Lys-Gly-Gly-D-threo-(OH)Asp-D-Glu-D-Ser-L-Ala-D-Ala-D-Ala-L-Ala-L-N5-(OH)Orn.According to the “short-hand” nomenclature proposed in [2]*** the two compounds should be characterized as pyoverdin-Q-akGGd'qsAaaAO′*-SUCA and pyoverdin-Q-akGGd'qsAaaAO′ *-SUC

Structure Elucidation of Azotobactin 87, Isolated from Azotobacter vinelandii ATCC 12837*, **

1996 ◽  
Vol 51 (3-4) ◽  
pp. 139-150 ◽  
Author(s):  
E. M. Schaffner ◽  
R. Hartmann ◽  
K. Taraz ◽  
H. Budzikiewicz
Keyword(s):  
Structure Elucidation ◽  
Culture Medium ◽  
Azotobacter Vinelandii ◽  
2D Nmr ◽  
Chemical Degradation ◽  
Spectroscopic Methods ◽  
Hydroxybutyric Acid ◽  
Iron Deficient ◽  
N Terminus ◽  
Sequential Information

Abstract Chromopeptide siderophores (azotobactin 87-1 and -II) were isolated from an iron deficient culture medium of Azotobacter vinelandii ATCC 12837 (=DSM 87). Their structures were elu­ cidated by chemical degradation studies and spectroscopic methods, especially 2D-NMR-tech-niques. Total assignments of 1H-, 13C-, and 15N-resonances based on 2D-HOHAHA-, 1H/13C-HMQC-, 1H /13C-HMBC-, 1H /15N-HMQC/TOCSY-, and 1H/15N-HMBC-experiments are given as well as sequential information derived from 1H/1H-NOESY-, 1H /13C-HMBC-and 1H/ 13N-HMBC-experiments. Both Az 87-1 and Az 87-11 consist of a tetracyclic chromophore -(1S)8,9-dihydroxy-4-oxo-2,3,4,5-tetrahydro-1H,10cH-3a,5,10b-triazaacephenantrylene-1-carb-oxylic acid -and a decapeptide chain linked with the N-terminus to the carboxy group of the chromophore containing also modified, non-proteinogenic amino acids. The sequence L-Ser-D-Ser-L-Hse-Gly-D-threo-OHAsp-Hse-Hse-Hse-D-N5OH-N5-R-Hbu-Om-L-Hse was determined for Az 87-1, while Az 87-11 contains a C-terminal L-Hse-lactone instead. Iron is chelated by the catecholic group of the chromophore, the β-hydroxy aspartic acid, and the hydroxamate function formed by N5-hydroxyornithine and R-β-hydroxybutyric acid.

Fate of Safening Agent L-2-Oxothiazolidine-4-Carboxylic Acid in Sorghum (Sorghum bicolor)

Weed Science ◽  
1990 ◽  
Vol 38 (3) ◽  
pp. 201-205 ◽  
Author(s):  
James L. Hilton ◽  
Parthasarathy Pillai ◽  
Helen A. Norman
Keyword(s):  
Carboxylic Acid ◽  
Sorghum Bicolor ◽  
Culture Medium ◽  
In Vitro Assay ◽  
Thiol Compounds ◽  
Vitro Assay ◽  
Herbicide Safener ◽  
Liquid Culture Medium ◽  
Germinating Seeds

The herbicide safener OTC (L-2-oxothiazolidine-4-carboxylic acid) increased the amount of reduced thiol compounds in sorghum [Sorghum bicolor(L.) Moench. ‘DK 427′] seedlings. When seedlings were grown in liquid culture medium containing35S-OTC, the compound was metabolized to radiolabeled cysteine and glutathione. The addition of tridiphane [2-(3,5-dichlorophenyl)-2-(2,2,2-trichloroethyl)oxirane] increased conversion of35S-OTC to cysteine and resulted in the formation of one additional35S-labeled compound. When35S-glutathione was injected into germinating seeds it was converted to35S-cysteine and both thiols were subsequently found in roots and shoots. Seeds injected with35S-OTC both translocated the compound to developing roots and shoots and metabolized35S-OTC to cysteine and glutathione. Excised roots and shoots also metabolized35S-OTC to the thiols. In an in vitro assay the enzyme 5-oxoprolinase converted OTC to cysteine.

Zur Genese Der Amidisch An Den Chromophor Von Pyoverdinen Gebundenen Dicarbonsäuren [1]

1991 ◽  
Vol 46 (5-6) ◽  
pp. 398-406 ◽  
Author(s):  
H. Schäfer ◽  
K. Taraz ◽  
H. Budzikiewicz
Keyword(s):  
Glutamic Acid ◽  
Dicarboxylic Acid ◽  
Succinic Acid ◽  
Pseudomonas Fluorescens ◽  
Exponential Growth ◽  
Culture Medium ◽  
Culture Time ◽  
Hydrolysis Of

Pseudomonas strains of the so-called fluorescent group usually produce several pyoverdins which differ only in the nature of a dicarboxylic acid bound amidically to the chromophor. For the pyoverdins isolated from the culture medium of Pseudomonas fluorescens 12 it is shown that succinic acid is an artefact formed by hydrolysis of succinic amide, and that a-ketoglutaric acid is transformed enzymatically to glutamic acid. This process is reversed after the phase of exponential growth of the bacteria. The ratio C4- vs. C5 -acids changes with the culture time and with increasing Fe3+ content of the medium in favor of the latter

Purification and Characterization of Three Extracellular Proteinases Produced by Pseudomonas fluorescens INIA 745, an Isolate from Ewe's Milk

1999 ◽  
Vol 62 (5) ◽  
pp. 543-546 ◽  
Author(s):  
J. FERNÁNDEZ ◽  
A. F. MOHEDANO ◽  
P. GAYA ◽  
M. MEDINA ◽  
M. NUÑEZ
Keyword(s):  
Pseudomonas Fluorescens ◽  
Culture Medium ◽  
Inhibitory Effect ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Purification And Characterization ◽  
Ph Optimum ◽  
Extracellular Proteinases ◽  
Ewe's Milk

Three proteinases were isolated from culture medium of Pseudomonas fluorescens INIA 745 and purified to homogeneity by a combination of Phenyl-Sepharose, DEAE-Sepharose, and Sephadex G-100 chromatography. Optimal temperature for enzymatic activity was 45°C for all three proteinases. The pH optimum of proteinases I and II was found to be 7.0, while that of proteinase III was 8.0. Divalent metal ions like Cu2+, Co2+, Zn2+, Fe2+, and Hg2+ were inhibitory to proteinase activity while Ca2+, Mg2+, and Mn2+ had little or no inhibitory effect. The three enzymes were strongly inhibited by EDTA and 1,10-phenantroline and partially by cysteine. The three enzymes are metalloproteinases since they were inhibited by chelators and reactivated by Co2+, Mn2+, Cu2+, and Zn2+. The Km values of proteinases I, II, and III for casein were calculated to be 3.2, 2.6, and 5.2 mg/ml, respectively. Proteinases II and III rapidly degraded β-casein, with preference to αs1-casein, whereas proteinase I hydrolyzed both casein fractions at a slow rate.

scholarly journals Characterization of Pit, a Streptococcus pneumoniae Iron Uptake ABC Transporter

2002 ◽  
Vol 70 (8) ◽  
pp. 4389-4398 ◽  
Author(s):  
Jeremy S. Brown ◽  
Sarah M. Gilliland ◽  
Javier Ruiz-Albert ◽  
David W. Holden
Keyword(s):  
Streptococcus Pneumoniae ◽  
Abc Transporter ◽  
Iron Uptake ◽  
Systemic Infection ◽  
Iron Chelator ◽  
Iron Deficient ◽  
Deficient Medium ◽  
Mutant Strains

ABSTRACT Bacteria frequently have multiple mechanisms for acquiring iron, an essential micronutrient, from the environment. We have identified a four-gene Streptococcus pneumoniae operon, named pit, encoding proteins with similarity to components of a putative Brachyspira hyodysenteriae iron uptake ABC transporter, Bit. An S. pneumoniae strain containing a defined mutation in pit has impaired growth in medium containing the iron chelator ethylenediamine di-o-hydroxyphenylacetic acid, reduced sensitivity to the iron-dependent antibiotic streptonigrin, and impaired virulence in a mouse model of S. pneumoniae systemic infection. Furthermore, addition of a mutation in pit to a strain containing mutations in the two previously described S. pneumoniae iron uptake ABC transporters, piu and pia, resulted in a strain with impaired growth in two types of iron-deficient medium, a high degree of resistance to streptonigrin, and a reduced rate of iron uptake. Comparison of the susceptibilities to streptonigrin of the individual pit, piu, and pia mutant strains and comparison of the growth in iron-deficient medium and virulence of single and double mutant strains suggest that pia is the dominant iron transporter during in vitro and in vivo growth.

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