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Xanthobacter autotrophicus

Janssen DB, A Scheper, L Dijkhuizen, B Witholt (1985) Degradation of halogenated aliphatic compounds by Xanthobacter autotrophicus GJIO. Appl Environ Microbiol 49 673-677. [Pg.329]

Sluis MK, RA Larsen, JG Krum, R Anderson, WW Metcalf, SA Ensign (2002) Biochemical, molecular, and genetic analyses of the acetone carboxylases from Xanthobacter autotrophicus strain Py2 and Rhodo-bacter capsulatus strain BIO. J Bacteriol 184 2969-2977. [Pg.334]

FIGURE 7.62 Degradation of 1,2-dichloroethane by Xanthobacter autotrophicus strain GJIO. (From Neilson, A.H. and Allard, A.-S., The Handbook of Environmental Chemistry, Vol. 3R, pp. 1-74, Springer, 2002. With permission.)... [Pg.361]

Keuning S, DB Janssen, B Witholt (1985) Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ 10. J Bacterial 163 635-639. [Pg.373]

Kinetic isotope effects for the dechlorination by Xanthobacter autotrophicus strain GJIO were 1.0045 for 1,2-dichloroethane, and 1.0066 for 1-chlorobutane (Lewandowicz et al. 2001). [Pg.633]

Fig. 11.4. Catalytic cycle of the haloalkane dehalogenase of Xanthobacter autotrophicus... [Pg.695]

Molecular dynamics simulations of ground and transition states have been carried out for the n2 displacement of chloride ion from 1,2-dichloroethane by the Asp 124-C02 at the active site of Xanthobacter autotrophicus haloalkane dehalogenase. ... [Pg.344]

Xanthobacter autotrophicus Halogenated compounds degradation, depollution Erable et al., 2005, 2006 [15,16]... [Pg.257]

Figure 12-1 The active site structure of haloalkane dehalogenase from Xanthobacter autotrophicus with a molecule of bound dichloroethane. See Pries et al.13 The arrows illustrate the initial nucleophilic displacement. The D260 - H289 pair is essential for the subsequent hydrolysis of the intermediate ester formed in the initial step. Figure 12-1 The active site structure of haloalkane dehalogenase from Xanthobacter autotrophicus with a molecule of bound dichloroethane. See Pries et al.13 The arrows illustrate the initial nucleophilic displacement. The D260 - H289 pair is essential for the subsequent hydrolysis of the intermediate ester formed in the initial step.
Whole-cell enantioselective oxidation of sulfides is in fast development and of preparative interest. Additional examples with Acinetobacter sp NCIMB 9871, Pseudomonas sp. NCIMB 9872, and Xanthobacter autotrophicus DSM 431 have been reported [113,114]. [Pg.350]

Lightstone FC, Zheng Y-J, Bruice TC (1998) Molecular Dynamics Simulations of Ground and Transition States for the SN2 Displacement of CL from 1,2-Dichloroethane at the Active Site of Xanthobacter autotrophicus Haloalkane Dehalogenase. J Am Chem Soc 120 5611... [Pg.495]

Fig. 12.4. Scanning electron micrograph showing calcium carbonate crystals found (A) associated with a Xanthobacter autotrophicus culture on an acetate-rich medium, (B) on the same medium with Ralstonia eutropha, (C) with the same bacterium on a citrate-rich medium and (D) on the same medium with Xanthobacter autotrophicus. Fig. 12.4. Scanning electron micrograph showing calcium carbonate crystals found (A) associated with a Xanthobacter autotrophicus culture on an acetate-rich medium, (B) on the same medium with Ralstonia eutropha, (C) with the same bacterium on a citrate-rich medium and (D) on the same medium with Xanthobacter autotrophicus.
The following proteins were chosen for multiple sequence alignment T. califomica acetylcholinesterase, Xanthobacter autotrophicus haloalkane dehalogenase, G. candidum lipase and wheat serine carboxypeptidase. This set was selected because they are all members of the o/fi hydrolase fold family (Ollis et al, 1992). This family of proteins, which is believed to have evolved by... [Pg.658]

It is well established that the same three-dimensional scaffolding in proteins often carries constellations of amino acids with diverse enzymatic functions. A classic example is the large family of a/jS, or TIM, barrel enzymes (Farber and Petsko, 1990 Lesk et ai, 1989). It appears that lipases are no exception to date five other hydrolases with similar overall tertiary folds have been identified. They are AChE from Torpedo calif arnica (Sussman et al., 1991) dienelactone hydrolase, a thiol hydrolase, from Pseudomonas sp. B13 (Pathak and Ollis, 1990 Pathak et al, 1991) haloalkane dehalogenase, with a hitherto unknown catalytic mechanism, from Xanthobacter autotrophicus (Franken et al, 1991) wheat serine carboxypeptidase II (Liao et al, 1992) and a cutinase from Fusa-rium solani (Martinez et al, 1992). Table I gives some selected physical and crystallographic data for these proteins. They all share a similar overall topology, described by Ollis et al (1992) as the a/jS hydrolase... [Pg.33]

Vanabins, storage proteins for the vanadyl cation found in ascidians, and containing up to 20 VO + attached to amine terminals of lysines (section 4.1.2 and Figure 4.4). A vanadium(IV)-binding protein was also isolated from the bacterium Pseudomonas isachenkovii (Section 4.5) which utilises vanadate as terminal electron acceptor in anaerobic respiration, and appears as well to be present in the hydrogen bacterium Xanthobacter autotrophicus. ... [Pg.182]

Ridder, IS., Rozeboom, H.J., and Dijkstra, B.W. (1999) Haloalkane dehalogenase from Xanthobacter autotrophicus GJIO refined at 1.15 A resolution, Acta Cryst. D55, 1273-1290. [Pg.287]

Haloalkane dehalogenase from Xanthobacter autotrophicus GJIO exhibits a solvent isotope effect of 3 and linear proton inventories for k for hydrolysis of dibrome-thane and 1,2-dichloroethane [58]. Stopped-flow fluorescence experiments under single-turnover conditions suggest that halide release limits k. This isotope effect was interpreted to reflect a conformational change of the protein that allows departure of halide. [Pg.1469]

Xanthobacter autotrophicus French pressure cell DEAE-cellulose Sephadex... [Pg.6]

Cp, Clostridium pasteurianum Bp, Bacillus polymyxa Kp, Klebsiella pneumoniae Rr, Rhodospirillum rubrum Ac, Azotobacter chroococcum Xa, Xanthobacter autotrophicus Rj, Rhizobium japonicum Rl, Rhizobium leguminosarum bacteroids. [Pg.9]


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