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Zoogloea ramigera

The 3-ketothiolase has been purified and investigated from several poly(3HB)-synthesizing bacteria including Azotobacter beijerinckii [10], Ral-stonia eutropha [11], Zoogloea ramigera [12], Rhodococcus ruber [13], and Methylobacterium rhodesianum [14]. In R. eutropha the 3-ketothiolase occurs in two different forms, called A and B, which have different substrate specificities [11,15]. In the thiolytic reaction, enzyme A is only active with C4 and C5 3-ketoacyl-CoA whereas the substrate spectrum of enzyme B is much broader, since it is active with C4 to C10 substrates [11]. Enzyme A seems to be the main biosynthetic enzyme acting in the poly(3HB) synthesis pathway, while enzyme B should rather have a catabolic function in fatty-acid metabolism. However, in vitro studies with reconstituted purified enzyme systems have demonstrated that enzyme B can also contribute to poly(3HB) synthesis [15]. [Pg.128]

Masamune, S., Palmer, M.A.J., Gamboni, R., Thompson, S., Davis, J.T., Williams, S.F., Peoples, O.P., Sinskey, A.J., and Walsh, C.T. (1989) Bio-Claisen condensation catalyzed by thiolase from Zoogloea ramigera. Active site cysteine residues. Chemtracts Org. Chem. 2, 247-251. [Pg.1092]

Norberg, A. B. and Persson, H. (1984). Accumulation of heavy metals by Zoogloea ramigera, Biotechnol. Bioeng., 26, 239-246. [Pg.518]

Kuhn, S. P. and Pfister, R. M. (1989). Adsorption of mixed metals and cadmium by calcium alginate immobilised Zoogloea ramigera, Appl. Microbiol., 31, 613-618. [Pg.519]

Ethyl (R)-3-hydroxybutanoate (15) of 100% e.e. is prepared by ethanolysis of poly-3-hydroxybutanoate (PHB) (16,1/7). Seebach et al. used PHB generated by Alcaligenes eutrophus (16), while we employed Zoogloea ramigera(15,17). [Pg.338]

Davis JT, Moore RN, Imperiali B, Pratt AJ, Kobayashi K, Masamune S, Sinskey AJ, Walsh CT, Eukni T, Tomita K. Biosynthetic thiolase from zoogloea-ramigera.1. Prehminary characterization and analysis of proton-transfer reaction. J. Biol. Chem. 1987 262 82-89. [Pg.243]

Palmer MAJ, Differding E, Gamboni R, Williams SF, Peoples OP, Walsh CT, Sinskey AJ, Masamune S. Biosynthetic thiolase from zoogloea-ramigera. Evidence for a mechanism involving Cys-378 as the active-site base. J. Biol. Chem. 1991 266 8369-8375. [Pg.244]

Tanaka, T., Hirama, M. Bio-Claisen condensation catalyzed by thiolase from Zoogloea ramigera. Active site cysteine residues. Chemtracts Org. Chem. 1989, 2, 247-251. [Pg.559]

Scheme 9 (a) The general mechanism of decarboxylating and nondecarboxylating Clalsen condensing enzymes, (b) A mechanistic proposal for the thiolase enzyme from Zoogloea ramigera as based on Its determined crystal structure. [Pg.393]

The Poly-3-hydroxybutyrate (P3HB) form of PHB [54, 55, 4, 56, 57] is probably the most common type of polyhydroxyalkanoate which is isolated from Azotobacter chroococcum. Pseudomonas putida. Pseudomonas oleovorans, Alcaligenes eutrophus, Zoogloea ramigera, and Alcaligenes sp. A-04 [ 58, 59, 55,60, 61,62,56]. [Pg.300]

Peoples O.P., Masamune S., Walsh C.T. and Sinskey A.J., 1987, Biosynthetic thiolase from Zoogloea ramigera. III. Isolation and characterization of the structural gene. J. Biol. Chem. 262 97-102. [Pg.166]

Logan, B. E. and Wilkerson, D. B. (1991). Eractal dimensions and porosities of Zoogloea ramigera and Saccharomyces cerevisae aggregates. Biotechnol. Bioeng., 23, 389-396. [Pg.110]

Fractal dimensions of both bacteria and yeast fiocs have also been determined in liquid culture in the laboratory, providing a useful quantification of fluid dynamic environment effects upon microbial aggregates. The bacterium Zoogloea ramigera had a A = 1-69 0.11 (determined from projected area. Section 8.2.4)... [Pg.247]


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See also in sourсe #XX -- [ Pg.753 ]

See also in sourсe #XX -- [ Pg.689 , Pg.690 ]

See also in sourсe #XX -- [ Pg.689 , Pg.690 ]

See also in sourсe #XX -- [ Pg.57 , Pg.84 , Pg.89 , Pg.90 , Pg.91 , Pg.98 , Pg.129 , Pg.136 , Pg.313 , Pg.320 ]




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