Oxidative Pseudomonas putida

Methylpyrazine-2- Acipimox Anti-lipolytic Oxidation Pseudomonas putida Single-stage fermentation [6]... 

The oxidation by strains of Pseudomonas putida of the methyl group in arenes containing a hydroxyl group in the para position is, however, carried out by a different mechanism. The initial step is dehydrogenation to a quinone methide followed by hydration (hydroxylation) to the benzyl alcohol (Hopper 1976) (Figure 3.7). The reaction with 4-ethylphenol is partially stereospecific (Mclntire et al. 1984), and the enzymes that catalyze the first two steps are flavocytochromes (Mclntire et al. 1985). The role of formal hydroxylation in the degradation of azaarenes is discussed in the section on oxidoreductases (hydroxylases). 

The oxidation of f-butyl methyl ether to f-butanol (Steffan et al. 1997), which is also mediated by the cytochrome P450 from camphor-grown Pseudomonas putida CAM, but not by that from Rhodococcus rhodochrous strain 116. 

Heald S, RO Jenkins (1994) Trichloroethylene removal and oxidation toxicity mediated by toluene dioxygenase of Pseudomonas putida. Appl Environ Microbiol 60 4634-4637. 

Rheinwald JG, AM Chakrabarty, C Gunsalus (1973) A transmissible plasmid controlling camphor oxidation in Pseudomonas putida. Proc Natl Acad Sci USA 70 885-889. 

Grund A, J Shapiro, M Fennewald, P Bacha, J Leahy, K Markbreiter, M Nieder, M Toepfer (1975) Regulation of alkane oxidation in Pseudomonas putida. J Bacteriol 123 546-556. 

Castro CE, NO Belser (1990) Biodehalogenation oxidative and reductive metabolism of 1,1,2-trichloroethane by Pseudomonas putida—biogeneration of vinyl chloride. Environ Toxicol Chem 9 707-714. 

Dunn NW, IC Gunsalus (1973) Transmissible plasmid coding early enzymes of naphthalene oxidation in Pseudomonas putida. J Bacteriol 114 974-979. 

Jeffrey AM, HJC Yeh, DM Jerina, TR Patel, JF Davey, DT Gibson (1975) Initial reactions in the oxidation of naphthalene by Pseudomonas putida. Biochemistry 14 575-584. 

The mandelate pathway in Pseudomonas putida involves successive oxidation to benzoyl formate and benzoate, which is further metabolized via catechol and the 3-ketoadipate pathway (Figure 8.35a) (Hegeman 1966). Both enantiomers of mandelate were degraded through the activity of a mandelate racemase (Hegeman 1966), and the racemase (mdlA) is encoded in an operon that includes the next two enzymes in the pathway—5-mandel-ate dehydrogenase (mdlB) and benzoylformate decarboxylase (mdlC) (Tsou et al. 1990). 

Mutations at the active site of CYPlOl (cytochrome P450j,j jj) from a strain of Pseudomonas putida made possible the monooxygenation of chlorinated benzenes with less than three substituents to chlorophenols, with concomitant NIH shifts for 1,3-dichlorobenzene (Jones et al. 2001). Further mutations made it possible to oxidize even pentachlorobenzene and hexachlorobenzene to pentachlorophenol (Chen et al. 2002). Integration of the genes encoding cytochrome PTSO. into Sphingobium chlorophenolicum enabled this strain to partially transform hexachlorobenzene to pentachlorophenol (Yan et al. 2006). 

Smith CA, MR Flyman (2004) Oxidation of methyl tcrt-butyl ether by alkane hydroxylase in dicyclopro-pyUcetone-induced and n-octane-grown Pseudomonas putida Gpol. Appl Environ Microbiol 70 4544-4550. 

The oxidation of morphine by Pseudomonas putida MIO gave rise to a large number of transformation products including hydromorphone (dihy-dromorphinone), 14/3-hydroxymorphine, 14 6-hydroxymorphinone, and dihydromorphine. Similarly, in incubations with oxymorphone (14/3-hydroxy-... 

Schemes Transformation steps involved in the oxidation of morphine by incubation with Pseudomonas putida MIO, which gave hydromorphone (dihydromorphinone), 14 d-hydroxymorphine, 14 8-hydroxymorphinone, and dihydromorphine [52]...

Scheme 4 The initial steps in the metaholism of morphine and codeine hy Pseudomonas putida MIO involved in the oxidation process...

Benzene and other arenes can be oxidized to c -l,2-cyclohexadienediol enan-tiospecifically using a mutant of Pseudomonas putida through microbial techniques (equation 188)310. 

The catalyst efficiency of these hydroalumination varies from a turnover number (TON) of 20-91. It is possible that the catalyst is deactivated by the presence of oxygen and water. Examination of the 31P NMR spectrum of the catalyst indicates that the phosphine monoxide and dioxide are formed in the presence of nickel prior to the addition of the substrate. Rigorous exclusion of oxygen and water is necessary in all these reactions. The enantioselective nickel-catalyzed hydroalumination route to dihydronaphthalenols may prove to be particularly important. Only one other method has been reported for the enantioselective syntheses of these compounds microbial oxidation of dihydronaphthalene by Pseudomonas putida UV4 generates the dihydronaphthalenol in 60% yield and >95% ee.1... 

It has been known since the 1950s that benzene and its derivatives can be oxidized to the corresponding cyclohexadienols in the presence of Pseudomonas putida (see Scheme 8-4 for an example). 

Scheme 8-4. Oxidation of substituted benzene with Pseudomonas putida.

Bio-oxidation of bromobenzene 11 catalyzed by Pseudomonas putidae leads to diol 12. Protection of diol 12, followed by the addition of an acyl nitroso dienophile and subsequent reduction gives compound 14. This compound can be used as the key intermediate in the preparation of (+)-l-deoxy-galacto-nojirimycin (16) and related indolizidine compounds (15) (Scheme 8-5).12... 

Thus a number of enzymes have been shown to be able to control the oxidation of sulfides to optically active sulfoxides most extensive investigations have concentrated on mono-oxygenases (e.g. from Acinetobacter sp., Pseudomonas putida) and haloperoxidases1 071 (from Caldariomyces fumago and Coral I ina officinalis). A comparison of the methodologies11081 led to the conclusion that the haloperoxidase method was more convenient since the catalysts are more readily available (from enzyme suppliers), the oxidant (H2O2) is cheap and no cofactor recycling is necessary with the haloperoxidases. Typical examples of haloperoxidase-catalysed reactions are described in Scheme 24. 

The enzyme p-ethylphenol methylene hydroxylase (EPMH), which is very similar to PCMH, can also be obtained from a special Pseudomonas putida strain. This enzyme catalyzes the oxidation of p-alkylphenols with alkyl chains from C2 to C8 to the optically active p-hydroxybenzylic alcohols. We used this enzyme in the same way as PCMH for continuous electroenzymatie oxidation of p-ethylphenol in the electrochemical enzyme membrane reactor with PEG-ferrocene 3 (MW 20 000) as high molecular weight water soluble mediator. During a five day experiment using a 16 mM concentration of p-ethylphenol, we obtained a turnover of the starting material of more than 90% to yield the (f )-l-(4 -hydroxyphenyl)ethanol with 93% optical purity and 99% enantiomeric excess (glc at a j -CD-phase) (Figure 14). The (S)-enantiomer was obtained by electroenzymatie oxidation using PCMH as production enzyme. 

Aside from the multifaceted chemical conversions, there are sources to develop into industrially viable microbial conversions. 1,2,4-Butanetriol, for example, used as an intermediate chemical for alkyd resins and rocket fuels, is currently prepared commercially from malic acid by high-pressure hydrogenation or hydride reduction of its methyl ester. In a novel environmentally benign approach to this chemical, wood-derived D-xylose is microbially oxidized to D-xylonic acid, followed by a multistep conversion to the product effected by a biocatalyst specially engineered by inserting Pseudomonas putida plasmids into E. coli ... 

In an original application, Yasuda et al have used both l-AAO and d-AAO, and L-lysine oxidase to oxidize o ,Ci -diamino acids. The reactions produce the expected a-keto w-amino acid products, but these then spontaneously cyclize to form cyclic a-imino acids. These compounds are then substrates for the authors recently discovered A methyl amino acid dehydrogenase (NMAADH) from Pseudomonas putida, producing the pure L-cyclic amino acid (Scheme 5). 

The present reaction was proven to occur even when the microorganism had been grown on peptone as the sole carbon source. These results lead to the conclusion that this enzyme system is produced constitutively. In the case of man-delate-pathway enzymes in Pseudomonas putida, (S)-mandelate dehydrogenase was shown to be produced in the presence of an inducer (mandelic acid or benzoylformic acid) [5]. Thus, the expression of the present oxidizing enzyme of A. bronchisepticus is different from that of R putida. 

Biological. Robertson et al. (1992) reported that toluene dioxygenases from Pseudomonas putida FI and Pseudomonas sp. Strain JS 150 oxidized the methyl group forming 2-nitrobenzyl alcohol. 

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