Pseudomonas Structure

Deisenhofer J, Epp O, Miki K, Huber R and Michei H 1984 X-ray structure anaiysis of a membrane-protein compiex eiectron density map at 3 A resoiution and a modei of the chromophores of the photosynthetic reaction center from Rhode pseudomonas viridis J. Mol. Biol. 180 385-98... 

Boumann, U., et al. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa, a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 12 3357-3364, 1993. 

NMR spectra have been reported for the Rieske-type ferredoxins from Xanthobacter strain Py2 (88) and of toluene 4-monooxygenase from Pseudomonas mendocina (T4MOC) (88a) as well as for the water-soluble Rieske fragment from the bci complex of Paracoccus deni-trificans (ISFpd) (89). The spectra of these proteins are similar, which is consistent with the close structural relationship between the three proteins. In the reduced (paramagnetic) state, all three proteins show several hyperfine-shifted resonances between +83 and -16 ppm at 400 MHz or between 110 and +25 ppm at 300 MHz (Table X). 

The low-temperature method has been applied to some primary and secondary alcohols (Fig. 1) For example, solketal, 2,2-dimethyl-1,3-dioxolane-4-methanol (3) had been known to show low enantioselectivity in the lipase-catalyzed resolution (lipase AK, Pseudomonas fluorescens, E = 16 at 23°C, 27 at 0oc) 2ia however, the E value was successfully raised up to 55 by lowering the temperature to —40°C (Table 1). Further lowering the temperature rather decreased the E value and the rate was markedly retarded. Interestingly, the loss of the enantioselectivity below —40°C is not caused by the irreversible structural damage of lipase because the lipase once cooled below —40°C could be reused by allowing it to warm higher than -40°C, showing that the lipase does not lose conformational flexibility at such low temperatures. 

It is known that NHase used in industry has a lower optimum temperature," therefore many reports have been concerned with screening for thermostable NHase. Miyanaga et al. has succeeded to analyze the X-ray structure of such a thermostable NHase from Pseudomonas thermophila. Bacillus sp. BR449 producing NHase with optimum temperature of 55°C has been isolated. Similarly, Bacillus sp. RAPc8 has a growth optimum at 65°C. Takashima et al. has isolated Bacillus smithii strain SC-J05-1, with optimum temperature at 40°C, and whose NHase has an optimum temperature and pH of 50°C and 10, respectively. Its crystal structure has also been elucidated. Bacillus pallidus strain Dac521 has... 

Ruetschi U, B Odelhdg, S Lindstedt, J Barros-Soderling, B Persson, H Jornvall (1992) Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme. EurJ Biochem 205 459-466. 

Yamaguchi M, H Fujisawa (1982) Subunit structure of oxygenase components in benzoate 1,2-dioxygenase system from Pseudomonas arvilla C-1. J Biol Chem 257 12497-12502. 

Koenig K, JR Andreesen (1990) Xanthine dehydrogenase and 2-furoyl-coenzyme A dehydrogenase from Pseudomonas putida Ful two molybdenum-containing dehydrogenases of novel structural composition. J Bacteriol 172 5999-6009. 

The alkane hydroxylase belongs to a family of nonheme iron oxygenases. There is some structural similarity between the nucleotide sequence of the integral-membrane alkane hydroxylase and the subunits of the monooxygenase encoded by xylA and xylM in the TOL plasmid that are involved in hydrox-ylation of the methyl groups in toluene and xylene in Pseudomonas putida PaWl (Suzuki et al. 1991). 

Karthikeyan S, Q Zhou, Z Zhao, C-L Kao, Z Tao, H Robinson, H-w Liu, H Zhang (2004) Structural analysis of Pseudomonas 1-aminocyclopropane-l-carboxylate deaminase complexes insight into the mechanism of a unique pyridoxal-5 -phosphate dependent cyclopropane ring-opening reaction. Biochemistry 43 13328-13339. 

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. 

Nardi-Del V T, C Kutihara, C Park, N Esaki, K Soda (1997) Bacterial DL-2-haloacid dehalogenase from Pseudomonas sp. strain 113 gene cloning and structural comparison with D- and L-2-haloacid dehalogenases. J Bacterial 179 4232-4238. 

Poelarends GJ, R Saunier, DB Janssen (2001) fra 5-3-chloroacrylic acid dehalogenase from Pseudomonas pavonaceae 170 shares structural and mechanistic similarities with 4-oxalocrotonate tautomerase. J Bacteriol 183 4269-4277. 

Pseudomonas sp. strain P.J. 874 grown with tyrosine carried out dioxygenation of 4-hydroxyphenylpyruvate to 2,5-dihydroxyphenylacetate accompanied by an NIH shift (Lindstedt et al. 1977). The involvement of a high-spin ferric center coordinated with tyrosine is conclusively revealed in the primary structure of the enzyme (Riietschi et al. 1992). 

Kulakova AN, LA Kulakov, NY Akulenko, VN Ksenzenko, JTG Hamilton, JP Quinn (2001) Structural and functional analysis of the phosphonoacetate hydrolase (phnA) gene region in Pseudomonas fluorescens 23F. J Bacteriol 183 3268-3275. 

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