Enzyme pseudomonas

The redox coupling of the two hemes shows different degrees of complexity in these enzymes. Pseudomonas nautica (PnNiR) shows ideal behavior and values for heme c and heme d are -1-234 mV and +199 mV, respectively. " In contrast, PpNiR shows strong heme-heme interaction resulting in hysteretic behavior attributed to kinetically gated, conformationally dependent coopera-tit vity in two-electron transfer reactions. ... 

Today, heterogeneous catalysts used for biodiesel production (NaOH, KOH, CHO Na, and O, CH3OK) are cheap and readily available (Atapour Kariminia, 2011 Demirbas, 2011). Heterogeneous catalysts, such as solid catalysts (Ca (NO)/Al O, CaO/Al O Sr (N03)2/Zn0, ZrO/SO and zeolite HY, zeolite X) and enzymes Pseudomonas fluorescens, Rhizopus oryzae, Candida rugosa, and Pseudomonas cepacia), are currently applied for the production of biodiesel. 

Keto-3-deoxy-6>phosphogluconic add was first isolated as a product of the action of a bacterial enzyme (Pseudomonas sauharophyla) on 6-phos-phogluconic acid . It is also formed from ATP and 2-keto-3-deoxy-D-gluconic add with an enzyme from E. coli. ... 

The biosynthetic sequence for other aerobic bacteria appears, where known, to be similar to that in Pseudomonas dentrificans although the genes involved, and thus the enzymes, exhibit differences. 

Pefloxacin (33) is the N-methyl analogue of norfloxacin (58) and is at least partly converted to it by metabolic enzymes in vivo. It has been launched in France for the treatment of a number of infections including those caused by sensitive strains of Pseudomonas aeruginosa. It can be synthesized starting with the Gould-Jacobs reaction of 3-chloro-4-fluoroaniline (28) and diethyl ethoxymethylenemalonate in an addition-elimination sequence leading to 29 which undergoes... 

Further studies of Pseudomonas sp. lipase revealed a strong influence of the water content of the reaction medium (Entry 20) [48]. To be able to compare the enzyme activity and selectivity as a function of the water present in solvents of different polarities, it is necessary to use the water activity (a ) in these solvents. We used the... 

Fosfomycin is an antibiotic produced by several Streptomyces species [95, 96] as well as by the Gram-negative Pseudomonas syringiae and Pseudomonas viridiflava. dl, 98] As an analogue of phosphoenolpyruvate, it irreversibly inhibits UDP-N-acetylglu-cosamine-3-O-enolpymvyltransferase (MurA), the enzyme that catalyzes the first step in peptidoglycan biosynthesis [99]. 

In this process, penicillin G is first hydrolysed to 6-APA with the acylase derived from Kluyvera citwphila at a slightly alkaline pH (pH 75). Subsequently the 6-APA is incubated with an acylase derived from Pseudomonas mdanogenum and with DL-phenylglydne methyl ester at pH 55. This produces ampiciilin in reasonable yields only because of the specificity of the P. melanogenum enzyme. This enzyme does not react with penicillin G nor phenylacetic acid. 

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 isomerase (EC 5.3.3.1) from Pseudomonas testosteroni has been studied in detail. This enzyme transfers a hydrogen from position 4 to the 6fl-position. Although several isomerases have been detected, their presence is often seen as presenting problems as they frequently lead to product diversification. 

Nucleotidylation - the addition of adenylate-residues by Lnu enzymes - can also be the cause of resistance to lincosamide antibiotics in staphylococci and enterococci. A plasmid encoded ADP-ribosylating transferase (Arr-2) that leads to rifampicin resistance has been detected in various Enterobacteriaceae as well as in Pseudomonas aeruginosa. 

The first step in the complete biodegradation of primary alcohol sulfates seems to be the hydrolysis to yield alcohol. Sulfatases are able to hydrolyze primary alcohol sulfates. Different authors have isolated and used several sulfia-tase enzymes belonging to Pseudomonas species. The alcohol obtained as a result of the hydrolysis, provided that dehydrogenases have been removed to avoid the oxidation of the alcohol, was identified by chromatography and other methods [388-394]. The absence of oxygen uptake in the splitting of different primary alcohol sulfates also confirms the hydrolysis instead of oxidation [395, 396]. The hydrolysis may acidify the medium and stop the bacterial growth in the absence of pH control [397-399]. 

Of course, the influence of organic solvents on enzyme enantioselectivity is not limited to proteases but it is a general phenomenon. Quite soon, different research groups described the results obtained with lipases [28]. For instance, the resolution of the mucolytic drug ( )-trans-sobrerol (11) was achieved by transesteriflcation with vinyl acetate catalyzed by the lipase from Pseudomonas cepacia adsorbed on celite in various solvents. As depicted in Scheme 1.3 and Table 1.5, it was found that t-amyl alcohol was the solvent of choice in this medium, the selectivity was so high ( >500) that the reaction stopped spontaneously at 50% conversion giving both +)4rans-sobrerol and (—)-trans-sobrerol monoacetate in 100% optical purity [29]. 

However, whatever the mechanism of action is, the effect of solvents on enzyme selectivity is sometimes really dramatic. For example, Hrrose et al. [42] reported that in the Pseudomonas species lipase-catalyzed desymmetrization of prochiral... 

Enzyme-catalyzed stereoselective hydrolysis allows the preparation of enantio-merically enriched lactones. For instance. Pseudomonas sp. lipase (PSL) was found to be a suitable catalyst for the resolution of 5-undecalactone and 5-dodecalactone (Figure 6.20). Relactonization of the hydroxy acid represents an efficient method for the preparation of both enantiomers of a lactone [67]. 

Styrene was successfully oxidized to the S-product both by xylene monooxygenase from P. putida mt-2 [113] and styrene monooxygenase from Pseudomonas sp.VLB120 [114] (Scheme 9.13), with the latter enzyme displaying a particularly large substrate tolerance with excellent stereoselectivity (>99% ee). In this context it is interesting to note that both xylene monooxygenase as well as chloroperoxidase are very selective for mono-epoxidation in case of presence of multiple alkene functionalities [115]. 

The alkane hydroxylase from Pseudomonas oleovorans is particularly suitable for the epoxidation of terminal aliphatic double bonds and enables rapid access to the (3-blocker metoprolol (Scheme 9.14) [113,116]. Complementing this regioselectivity, chloroperoxidases are particularly suitable biocatalysts for the epoxidation of (ds substituted) subterminal olefins [112,117]. This enzyme also accepts terminal olefins and is utilized for the effident synthesis of P-mevalono-ladone [118]. 

For the kinetic resolution of racemic a-acetoxyamide 6 several native enzymes were used (Scheme 5.5). The native Upases from Pseudomonas cepacia (PCL) and porcine pancreas (PPL) showed the highesL although stiU unsatisfactory, enantios-electivity ( = 5.1 and 3.5, respectively). Upon immobilization into a solgel matrix, the enantioselectivity of PCL was improved significantly to 30.5. The covalent immobilization on Eupergit increased the enantioselectivity even more (34.0) [23]. 

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