Pseudomonas fluorescens, activity

C12H27N3O8 341.361 Aminoglycoside antibiotic. Isol. from Pseudomonas sorbicinii and Pseudomonas fluorescens. Active against grampositive and -negative bacteria. Sol. H2O fairly sol. MeOH, EtOH poorly sol. butanol, hexane. 

Specific information about the optimum conditions for the synthesis and the activity of the enzyme has been reported for Pseudomonas fluorescens screening of various micro-organisms resulted in the selection of a P. fluorescens strain with an initial rate of conversion of 3 g P h 1 in an imoptimised state. The following conclusions could be made concerning the production of L-phenylalanine by P. fluorescens ... 

The gene encoding the esterase from Pseudomonas fluorescens was expressed in Escherichia coli, and the enzyme displayed both hydrolytic and bromoperoxidase activity (Pelletier and Altenbnchner 1995). 

Siddiqui lA, D Haas, S Heb (2005) Extracellular protease of Pseudomonas fluorescens CHAO, a biocontrol factor with activity against the root-knot nematode Meloidogyne incognita. Appl Environ Microbiol 71 5646-5649. 

Recent studies have further examined the iron stress response of pseudomonads using an iron-regulated, ice-nucleation gene reporter (inaZ) for induction of the iron stress response (17,18,84). This particular reporter system was developed by Loper and Lindow (85) for study of microbial iron stress on plant surfaces but was later employed in soil assays. In initial. studies, cells of Pseudomonas fluorescens and P. syringae that contained the pvd-inaZ fusion were shown to express iron-responsive ice-nucleation activity in the bean rhizosphere and phyllosphere. Addition of iron to leaves or soil reduced the apparent transcription of the pvd-inaZ reporter gene, as shown by a reduction in the number of ice nuclei produced. 

Meickle, A et al. (1995) Matric potential and the survival and activity of a Pseudomonas fluorescens inoculum in soil. Soil Biology and Biochemistry, 27, 881-892. 

All bacteria where nitrate ester degradation has been characterized have very similar enzymes. The enzymes eatalyze the nicotinamide cofactor-dependent reductive eleavage of nitrate esters that produces alcohol and nitrite. Purification of the PETN reduetase from Enterobacter cloacae yielded a monomerie protein of around 40 kilo Daltons, which required NADPH as a co-faetor for aetivity. Similar enzymes were responsible for the nitrate ester-degrading activity in Agrobacterium radiobacter (Snape et al. 1997) - nitrate ester reductase - and in the strains of Pseudomonas fluorescens and Pseudomonas putida (Blehert et al. 1999) - xenobiotic reduetases . All utilize a non-covalently bound flavine mononucleotide as a redox eofactor. 

It is nearly 50 years since a c-type cytochrome was shown to catalyze peroxidase activity in crude extracts of Pseudomonas fluorescens (40). The enzyme responsible was first purified some 20 years later by Ell-folk and Soninen from the closely related P. aeruginosa and shown to be a diheme cytochrome c peroxidase (CCP) (41). These bacterial diheme CCPs are quite distinct from the superfamily of plant and yeast peroxidases (42) and are widely distributed among the Gram-negative bacteria (41, 43 6). Diheme CCPs are located in the periplasm (Fig. 2), where they catalyze the two-electron reduction of H2O2 to H2O by soluble one-electron donors such as cytochromes c and cupredoxins. 

Pseudomonas fluorescens periplasmic, active on 4-methylumbelliferyl p-D-cellobioside 55... 

This group comprises condensation products of salicylic acid with cysteine giving a thiazoline ring. For a review, see (570). Some structurally related compounds will also be mentioned here. Salicylic acid isolated from Burkholderia Pseudomonas) cepacia was named azurochelin (555). It was found to act as a siderophore, e.g. for Pseudomonas fluorescens (230) and P. syringae (178) see also Mycobacterium smegmatis (Sect. 2.8). For details on the siderophore activity of salicylic acid, see (559). 

Anthoni U, Christophersen C, Nielsen PH, Gram L, Petersen BO (1995) Pseudomonine, an Isoxazolidone with Siderophoric Activity from Pseudomonas fluorescens AH2 Isolated from a Lake Victorian Nile Perch. J Nat Prod 58 1786... 

Naturally derived from fermentation using Pseudomonas fluorescens and active against MRSA and some other grampositive bacteria. Acts by blocking the activity of isoleucyl-tRNA synthetase in bacteria. This enzyme is necessary for bacteria to synthesize proteins. 

The first enzymatic polymerizations of substituted lactones were performed by Kobayashi and coworkers using Pseudomonas fluorescens lipase or CALB as the biocatalyst [90-92]. A clear enantiopreference was observed for different lactone monomers, resulting in the formation of optically active polymers. More recently, a systematic study was performed by Al-Azemi et al. [93] and Peelers et al. [83] on the ROP of 4-alkyl-substituted CLs using Novozym 435. Peelers et al. studied the selectivity and the rates as a function of the substituent size with the aim of elucidating the mechanism and the rate-determining step in these polymerizations. Enantio-enriched polymers were obtained, but the selectivity decreased drastically with the increase in substituent size [83]. Remarkably for 4-propyl-e-caprolactone, the selectivity was for the (R)-enantiomer in a polymerization, whereas it was S)-selective in the hydrolysis reaction. Comparison of the selectivity in the hydrolysis reaction (Fig. 10b) with that of the polymerization reaction (Scheme 8a) revealed that the more bulky the alkyl substituent, the more important the deacylation step becomes as the rate-determining step. 

Compound (XIV) was the most activity against Pseudomonas fluorescens, an organism that Is not affected by the potent photosensitizer 8-methoxypsoralen (27). The three compounds were active against Saccharomyces cerevlslae and Candida albicans. 

The work of Ye et al. (1991) was extended to include Tn5 mutants in nir genes for nitrite reductase of Pseudomonas fluorescens (Ye etal., 1992a) and Pseudomonas sp. strain G-179 (Ye et al., 1992b) which use, respectively, the cytochrome cd - and Cu-type nitrite reductase. The five mutants of P. fluorescens characterized not only lacked nitrite reductase and N0/H20- 0 exchange activities, but also showed levels of nitric oxide reductase activity that were diminished roughly by a factor of two. The reason for the decrease in nitric oxide reductase activity of the mutants is not clear, but may represent a change in... 

Bugg, T., J. M. Focht, M. A. Pickard, and M. R. Gray, Uptake and active efflux of polycyclic aromatic hydrocarbons by Pseudomonas fluorescens LP6a , Appl. Environ. Microbiol., 66, 5387-5392 (2000). 

Normander, B., Hendriksen, N.B., Nybroe, O. Green fluorescent protein-marked Pseudomonas fluorescens localization, viability, and activity in the natural barley rhizosphere. Appl Environ Microbiol 1999 65 4646-51. 

The lipase used was isolated from Pseudomonas fluorescens and was commercially available from Amano International Enzyme Co., Inc. (Troy, VA) as a powder, specific activity 32,000 units/g (P-30). 

Kojima, Y., Kobayashi, M., Shimizu, S. 2003. A novel lipase from Pseudomonas fluorescens HU380 Gene cloning, overproduction, renaturation-activation, two-step purification, and characterization. J. Biosci. Bioeng. 96, 242-249. 

Marin, A., Mawhinney, T.P., Marshall, R.T. 1984. Glycosidic activities of Pseudomonas fluorescens on fat-extracted skim milk, buttermilk and milk fat globule membranes. J. Dairy Sci. 67, 52-59. 

Owusu, R.K., Makhzoum, A., Knapp, J.S. 1992, Heat inactivation of lipase from psychrotrophic Pseudomonas fluorescens P38 Activation parameters and enzyme stability at low or ultra high temperature. Food Chem. 44, 261-268. 

A brief report has appeared in which a wild-type esterase from Pseudomonas fluorescens (PFE), which shows no activity in the hydrolysis of the ester 16 (Fig. 11.21), was subjected to mutagenesis using the mutator strain Epicurian coli XL 1-Red [83], This resulted in a variant which catalyzes the reaction with an ee of 25 %. The absolute configuration of the major product ((R)- or (S)-17) was not determined. Sequencing of the esterase-variant revealed that two point mutations, A 209D and L181V, had occurred. Since the structure of the enzyme is unknown, a detailed interpretation was not possible, although reasonable speculations were made. 

Pseudomonas fluorescens esterase MS growth/ pH-indicator active double mutant acting on sterically hindered substrate 22, 24, 26... 

Scheme 14.3. Principle of the assay system used to identify active variants of esterase from Pseudomonas fluorescens (PFE) acting on the sterically hindered 3-hydroxy ester 1. Both substrates 1a,b yield the free acid leading to a color change 1b also releases the carbon source glycerol leading to enhanced growth of esterase mutant producing E. coli clones.

Dorr, P. and Knowles, C. 1989. Cyanide oxygenase and cyanase activities of Pseudomonas fluorescens NCIMB 11764. FEMS Microbiology Letters, 60 289-94. 

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