Bacillus subtilis enzymes

Pitkanen, K., Heikinheimo, R. and Pakkanen, R. (1992) Purification and characterization of Erwinia chrysanthemi B374 pectin methylesterase produced by Bacillus subtilis. Enzyme Microb TechnoHA, 832-836. 

P. S. J. Cheetam, A. J. Hacking, and M. Vlitos, Synthesis of novel disaccharides by a newly isolated fructosyltransferase from Bacillus subtilis, Enzyme Microb. Technol., 11 (1989) 212-219. 

Kast P, M Asif-Ullah, D Hilvert (1996) Is chorismate mutase a prototypic entropy trap Activation parameters for die Bacillus subtilis enzyme. Tetrahedron Lett. 37 (16) 2691—2694... 

Dust suppression other ways of suppressing dust, e.g. using Bacillus subtilis enzyme in a granular, rather than a powder, form... 

JUNIPER, C.P., HOW, M.J., GOODWIN, B.F.J. KINSHOTT, A.K. (1977) Bacillus subtilis enzymes a 7 year clinical, epidemiological and immunological study of an industrial allergen. Journal of the Society of Occupational Medicine, 27, 3-12. 

Bacillus subtilis (enzyme expression is induced by sulfur, nitrogen or carbon starvation [8]) [8]... 

Based on the crystal structure of the Bacillus subtilis enzyme in complex with product UMP, Appleby and associates have proposed a novel, electrophilic substitution mechanism for the ODCase reaction (Fig. 3d) [26]. Instead of requiring the formation of a discrete carbanion in the transition state for decarboxylation, this mechanism postulates that Lys-93 protonates... 

Steinmetz, M. LeCoc, D., Aymerich, S., Gonzy Trdboul, G. and Gay, P., 1985, The DNA sequence of the gene for the secreted Bacillus subtilis enzyme levansucrase and its genetic control sites. Mol. Gen. Genet., 200 220. 

Detergent workers disease Detergent Bacillus subtilis, enzymes... 

A comparison of the structures of penicillin and Dalanyl-Dalanine (cf. structures 41 and 42) shows that there is a great deal of similarity between the two molecules. Penicillin is essentially an acylated cyclic dipeptide of Dcysteine and Dvaline (84). As such, it contains a peptide bond, that of the /3-lactam ring, that can acylate the enzyme. Labeling studies of the peptidoglycan transpeptidase of Bacillus subtilis indicate that radioactive penicillin reacts with a sulfhydryl group of a cysteine residue of the enzyme (86). 

However, to date, no AMA studies have been conducted against spore-forming microorganisms. It is very important to search for a compound having action on the development of such organisms as Bacillus subtilis and B. cereus, since these microorganisms are able to withstand pasteurization conditions and contain hydrolytic enzymes, which generate off-flavor in the food. 

The genes encoding the puc genes, which encode the enzymes in the aerobic pathway for the degradation of hypoxanthine, have been determined for Bacillus subtilis (Schultz et al. 2001), and involve the sequences (Figure 10.31) ... 

Kaminskas E, Y Kimhi, B Maganasik (1970) Urocanase and V-formrmino-L-glutamate formrminohy-drolase of Bacillus subtilis, two enzymes of the histidine degradation pathway. J Biol Chem 245 3536-3544. 

DNA polymerase I has been purified to homogeneity. When the pure enzyme is treated with subtilisin, a proteolytic enzyme from Bacillus subtilis, the polymerase is cleaved into two pieces. The small fragment retains the 5 to 3 nuclease activity, whereas the larger piece, called a Klenow fragment, has both polymerase activity and the 3 to 5 exonuclease activity. The Klenow fragment is sold commercially for use in labeling DNA for use in detecting recombinant DNA. 

Ohshiro, T. Ishii, Y. Matsubara, T., et al., Dibenzothiophene Desulfurizing Enzymes From Moderately Thermophilic Bacterium Bacillus Subtilis WU-S2B Purification, Characterization and Overexpression. Journal of Bioscience and Bioengineering, 2005. 100(3) pp. 266-273. 

We routinely use a mix of five mRNAs that are derived from the lys (ATCC no. 87482), trp (ATCC no. 87485), dap (ATCC no. 87486), thr (ATCC no. 87484), andphe (ATCC no. 87483) clones from the bacterium Bacillus subtilis cloned into a vector that contains a stretch of As. These RNAs are generated by in vitro transcription using a T3 in vitro transcription kit (e.g., MEGAscript from Ambion) of the linearized DNA template with the appropriate restriction enzyme. 

Fischer, brilliant results were achieved, and in succession the a-amylases of pig pancreas, of Bacillus subtilis, of human saliva, of human pancreas, and of Aspergillus oryzae, and the /3-amylase of malt, were successfully crystallized. Important biological deductions were gained from this study whereas the amylases of human pancreas and saliva cannot be distinguished from one another, amylases from pig pancreas and from human pancreas are different. These differences are manifested in molecular weight, crystalline forms, electrophoretic mobility, and influence of the pH on the activity however, all the amylases have the same specific biochemical action. The identity of the enzymes seems to be dependent on the species and not on the organ. Interest in biologically active proteins led Meyer to a study of the protein hormones, a field in which he was very active at the time of his death. 

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