Pseudomonas oleovorans

C8Hi6-oxide Ketones C8H14 Pseudomonas oleovorans... 

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]. 

Timm Steinbuchel (1990) revealed the production of PHAs by Pseudomonas aeruginosa. It was found that when the cell reached to stationary phase, the intracellular PHAs were decreased. Lageveen et al (1998) produced PHAs from n-octane by Pseudomonas oleovorans. 

Formation of Polyesters by Pseudomonas oleovorans Effect of Substrates on Formation and Composition of Poly-(R)-3-Hydroxyalkanoates and Poly-(R)-3-Hydroxyalkenoates. Applied Environmental and Microbiology, 54, 2924-2932. 

Ruettinger RT, GR Griffith, MJ Coon (1977) Characteristics of the u-hydroxylase of Pseudomonas oleovorans as a non-heme iron protein. Arch Biochem Biophys 183 528-537. 

Pedrotta V, B Witholt (1999) Isolation and characterization of the cw/fra 5-unsaturated fatty acid isomerase of Pseudomonas oleovorans Gpol2. J Bacteriol 181 3256-3261. 

Epoxides may be formed from alkenes during degradation by Pseudomonas oleovorans, although octan-l,2-epoxide is not further transformed, and degradation of oct-l-ene takes place by co-oxidation (May and Abbott 1973 Abbott and Hou 1973). The co-hydroxylase enzyme is able to carry out either hydroxylation or epoxidation (Ruettinger et al. 1977). 

AbbottBJ, CT Hou (1973) Oxidation of 1-alkenes to 1,2-epoxides hy Pseudomonas oleovorans. ApplMicrobiol 26 86-91. 

Kok M, R Oldenius, MPG van der Linden, CHC Meulenberg, J Kingma, B Witholt (1989a) The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase. J Biol Chem 264 5442-5451. 

May SW, BJ Abbott (1973) Enzymatic epoxidation. II. Comparison between the epoxidation and hydroxyl-ation reactions catalyzed by the omega-hydroxylation system of Pseudomonas oleovorans. J Biol Chem 248 1725-1730. 

McKenna EJ, MJ Coon (1970) Enzymatic co-oxidation IV. Purification and properties of the co-hydroxylase of Pseudomonas oleovorans. J Biol Chem 245 3882-3889. 

The crystallographic structure of rubredoxin from Clostridium pasteurianum at 2.5 A, a resolution sufficient to reveal the sequence of several of the bulky amino acid side chains, shows the iron coordinated to two pairs of cysteine residues located rather near the termini of the polypeptide chain (Fig. 1). A related rubredoxin, with a three times larger molecular weight, from Pseudomonas oleovorans is believed to bind iron in a similar fashion. This conclusion is based on physical probes, especially electron paramagnetic resonance spectroscopy, all of which indicate that the iron is in each case situated in a highly similar environment however, the proteins display some specificity in catalytic function. 

Pyridyl-3-acetic acid 6 Risedronate Treatment for osteoporosis Oxidation Pseudomonas oleovorans Single-stage fermentation [7]... 

Keywords. Bacterial polyester, Medium-chain-length poly(3-hydroxyalkanoates), Pseudomonas oleovorans, Pseudomonas putida, Functional poly(3-hydroxyalkanoates), Short-chain-length poly(3-hydroxyalkanoates)... 

Ammonium Alcaligenes latus Pseudomonas oleovorans Pseudomonas cepacia Ralstonia eutrophus Rhodobacter sphaeroides Speudomonas sp. K. Methylocystus oarvus Thiosphaera pantotropha Rhizobium ORS 571... 

Potassium sulfate Bacillus thuringiensis Pseudomonas sp. K. Pseudomonas oleovorans Rho do spirillum rubrum Rhodobacter sphaeroids... 

Pseudomonas oleovorans (PhaC2) —Nocardia corallina ----Rhodococcus ruber PP2... 

Table 1. Monomer composition3 of PHAs produced by Pseudomonas oleovorans grown on n-alkanes as sole carbon and energy sourceb... 

Many Pseudomonas strains accumulate MCL-PHAs from alkane, alkene, al-kanoate, alkenoate, or alkanol [5,6,14,96]. The composition of the PHAs formed by the pseudomonads of the rRNA homology group I is directly related to the structure of the carbon substrate used [6]. These results suggested that MCL-PHAs are synthesized from the intermediates of the fatty acid oxidation pathway. In almost all pseudomonads belonging to the rRNA homology group I except Pseudomonas oleovorans, MCL-PHA can also be synthesized from acetyl-CoA through de novo fatty acid synthetic pathway [97]. The -oxidation pathway and de novo fatty acid synthetic pathway function independently in PHA biosynthesis. 

Second, some organisms are able to incorporate longer pendent chains yielding another class of PHA medium chain length PHA, poly(HAMCL). Poly (HAmcl) is specifically accumulated by fluorescent pseudomonads. When aliphatic hydrocarbons like n-alkane, n-alkanoate, or n-alkanol serve as feedstocks for Pseudomonas oleovorans the resulting PHA is a random copolymer... 

Schmid, A., Kollmer, A. and Witholt, B. (1998). Effects of biosurfactant and emulsification on two-liquid phase Pseudomonas oleovorans cultures and cell-free emulsions containing -decane, Enzyme Microb. Technol., 22, 487 -93. 

It is noteworthy that, in contrast to mammalian systems, the majority of bacterial strains exhibited sufficient activity even when the cells were grown under non-optimized conditions. Since enzyme induction is still a largely empirical task, cells were grown on standard media in the absence of inducers. Furthermore, all attempts to induce epoxide hydrolase activity in Pseudomonas aeruginosa NCIMB 9571 and Pseudomonas oleovorans ATCC 29347 by growing the cells on an alkane (decane) or alkene (1-octene) as the sole carbon source failed [27]. 

Another source of rubredoxins was found in an aerobic bacterium, Pseudomonas oleovorans, utilizing n-hexane as a carbon source (10). This particular rubredoxin differs from those commonly found in anaerobic bacteria in some of its properties it has a molecular weight of 19,000, and one iron form of the protein is readily converted to a two-iron form (11). The rubredoxin of P. oleovorans functions as a terminal electron transfer component in an enzyme system which participates in the ( -hydroxylation of fatty acids and hydrocarbons. The hydrocarbon-oxidizing... 

NADH NADH-iubredoxine reductase (fp), rubredoxin (NHI) NHI Pseudomonas oleovorans fatty acid-io-hydroxylase 43-45)... 

Nieboer, M., Kingma, J. Witholt, B. (1993). The alkane oxidation system of Pseudomonas oleovorans induction of the alk genes in Escherichia colt W3110 (pGEc47) affects membrane biogenesis and results in overexpression of alkane hydroxylase in a distant cytoplasmic membrane subfraction. Molecular Microbiology, 8, 1039-51. 

Eggink, G., Lageveen, R., Altenburg, B. Witholt, B. (1987a). Controlled and functional expression of the Pseudomonas oleovorans alkane utilizing system in Pseudomonas putida and Escherichia coli. Journal of Biological Chemistry, 262, 17 712-18. 

Two unusual rubredoxins are known at present, from D. gigas and Pseudomonas oleovorans. Both have two iron centres but differ from each other. The rubredoxin from D. gigas (desul-foredoxin) has a molecular weight of 7900, with no acid labile sulfide and eight cysteine residues.744 The electronic spectrum is different from that of the two-iron rubredoxin from P. oleovorans in that it is not simply the addition of two spectra of one-iron rubredoxins. These additional features have led to the suggestion that the two iron centres interact. 

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