Sporosarcina ureae

E. coli B. stearothermophilus., Sporosarcina ureae B. sphaeroides Phe dehydrogenase ... 

Regnlar arrays of platinnm were achieved by chemical reduction of a platinnm salt that had been deposited onto the S-layer of Sporosarcina ureae [132]. This S-layer exhibits sqnare lattice symmetry with a lattice constant of 13.2 nm. Transmission electron microscopy revealed the formation of well-separated metal clusters with an average diameter of 1.9 nm. Seven clnster sites per nnit cell were observed. UV-VIS spectrometry was nsed to study the growth kinetics of the clnsters. 

This enzyme [EC 1.4.1.20] catalyzes the reaction of l-phenylalanine with NAD and water to produce phenylpyruvate, ammonia, and NADH. The enzymes isolated from Bacillus badius and Sporosarcina ureae are highly specific for L-phenylalanine, whereas that isolated from Bacillus sphaericus also acts on L-tyrosine. 

A crystalline bacterial surface layer with a well defined geometry of Sporosarcina ureae (so-called S layer) is used as a protein template (unit cell 13.2 nm x 13.2 nm) on a cell membrane. Noble metal nanoclusters (Pt or Pd) are deposited chemically to produce nanostructures. The spatial distribution of noble metal nanoclusters is characterized by transmission electron microscopy (TEM). 

L-methionine DL-methionine + Asp a-keto-7-methylthiobutyric acid + NH4 + formic acid D-amino acid oxidase + transaminase Phe dehydrogenase + formate Trigonopsis variabilis Sporosarcina ureae 195... 

The use of so-called S-layers is a combination of self-organization and spatial patterning [88]. S-layers consist of 2-D protein crystals that are formed naturally as the outermost cell surface layer (S-layer) of prokaryotic organisms. The subunits can recrystallize into nanoporous monolayers in suspension, at liquid-surface interfaces, on lipid films, or on solid substrates. The S-layers of Bacillus sphaericus CCM 2177 have been used to generate ordered arrays of 4—5 nm gold particles, with a 13.1 nm repeat distance, from AuCr ions [89]. The spontaneous self-assembly of 5 nm AuN Ps was shown to occur at the S-layer of Deinococcus radiodurans, to produce micrometersized ordered domains [90]. Arrays of 1.9 nm platinum particles were achieved from Pt salts in the S-layer of Sporosarcina ureae [90] these were of square symmetry and had a lattice constant of 13.2 nm. 

The S-layer protein of Sporosarcina ureae ATCC 13881, observed for the first time in 1979, has not yet been fully characterized with respect to its selfassembling ability. Genetic and structural information exists, however in comparison to other S-layers, there is a lack of knowledge concerning the self-assembling structures it forms under different in vitro recrystallization conditions. Moreover, up to now, there are no data available on which part of the protein is responsible for its remarkable self-assembling property. 

Sporosarcina ureae ATCC 13881 is a Gram-positive, motile bacterium living in soil. Taxonomically, it belongs to the family of Bacillaceae under the genus Sporosarcina. It requires alkaline conditions for growth (pH 8.8 is optimal) and is able to form endo-spores (Goldman and Wilson, 1977 MacDonald and MacDonald, 1962). 

The native S-layer of Sporosarcina ureae ATCC 13881 was recrystallized at (a) low protein concentration (0.29 irg/jj, ) over a time period of 1 month, (b, c) higher protein concentration (0.79 [j,g/ij,l) over a time period of 12 days. 

Beveridge, TJ., 1979. Surface arrays on the wall of Sporosarcina ureae. J. Bacteriol. 139, 1039-1048. 

Goldman, M., Wilson, D.F., 1977. Growth of Sporosarcina ureae in defined media. FEMS Lett. 2, 113-115. 

Ryzhkov, P., 2007. Bioengineering of S-layers molecular characterization of the novel S-layer gene SslA of Sporosarcina ureae ATCC 13881 and nanotechnology application of SslA protein derivatives (Dissertation). TU Dresden. 

Ryzhkov, P., Ostermann, K., Rodel, G., 2007. Isolation, gene structure and comparative analysis of the S-layer gene sslA of Sporosarcina ureae ATCC 13881. Genetica 131, 255-265. 

Chapter 3, Self-assembly of nanobiomaterials, prepared by Varga et al., offers a recent review regarding the surface-layer proteins (S-layers) that represent a unique self-assembling system. Their remarkable property of self-assembling and their repetitive physicochemical properties down to the nanometer scale led to various applications in the fields of bio- and nanotechnology. Chapter 3 focuses on the basic principles and self-assembly properties of the S-layer protein of Sporosarcina ureae. 

S)-Amino-3-[3- 6-(2-methylphenyl) pyridyl]-propionic add 82a was prepared by an enzymatic deracemization process using a combination of two enzymes (P)-amino acid oxidase from Trigonopsis variabilis cloned and expressed in E. coli and an (S)-aminotransferase from Sporosarcina ureae, also cloned and expressed in E. coli [147]. Racemic amino acid 82 was used as a substrate and (S)-aspartate was used as amino donor. An (S)-aminotransferase was also purified from a soil organism identified as Burkholderia sp. and cloned and expressed in E. coli and used in this process [147]. This process was scaled up to 70 L scale. 

PheDH NAD Bacteria Sporosarcina ureae. Bacillus sphaericus, Rhodococcus marinas, Thermoactinomyces intermedius)... 

At the beginning of the 1980s, the wide screening of aromatic amino acid dehydrogenases led to the discovery of PheDH in Brevibacterium species [26]. The enzyme was isolated from several mesophiles—Bacillus sphaericus [27], Sporosarcina ureae [27], B. badius [28], Rhodococcus sp. [29], Nocardia sp. [30] and Microbacterium sp. [31], and also from the thermophile T. intermedius [32]—and characterize (Table 5). The enzyme acts on L-norleucine, L-methionine, L-norvaline, and L-tyrosine besides L-phenylalanine in the presence of NAD, although slowly. L-Tryptophan, L-alanine, and D-phenyManine are inert as the substrate. The enzyme shows lower substrate specificity for 2-oxo acids than that for amino acids like AlaDH and LeuDH. The values for ammonia are more than 70 mM. The T. intermedius PheDH is the most thermostable and a useful catalyst for industrial and clinical applications. The enzyme is easily and effectively purified from the recombinant E. coli [6] and commercially available (Unitika Ltd.). 

Similar methods have been used for the syntheses of L-phenylalanine and its analogs. An enzyme membrane reactor system containing Brevibacterium sp. PheDH, yeast FDH, and PEG-NADH was developed for the syntheses of L-phenylalanine from phenylpyruvate and ammonium formate [85]. Asano and Nakazawa synthesized L-phenylalanine, tyrosine, and some other L-amino acids using a dialysis tube containing the Sporosarcina ureae PheDH and yeast FDH [86]. In addition, optically pure three-substituted pyruvates with bulky substituents, such as 5 -2-amino-4-phenylbutyrate and 5-2-amino-5-phenylvalerate, were synthesized from their oxo analogs in a similar way [87]. 

---