Bacillus subtilis enzyme activity

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... 

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. 

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. 

In 1998 the long-known Bacillus subtilis inorganic pyrophosphatase was characterized and found to have much greater activity than the above enzymes, to have a completely different amino acid sequence, not to be inhibited by F and to be activated by This form of... 

Yet another proteolytic preparation used for debridement of wounds and skin ulcers consists of proteolytic enzymes derived from Bacillus subtilis. The preparation displays broad proteolytic activity and is usually applied several times daily to the wound surface. 

Mechanism of Action An antitubercular that inhibits DNA-dependent RNA polymerase, an enzyme in susceptible strains of Escherichia coli and Bacillus subtilis. Rifabutin has a broad spectrum of antimicrobial activity including against mycobacteria such as Mycobacterium avium complex (MAC). Therapeutic Effect Prevents MAC disease. 

It is commonly agreed that enzymes are inactive in nearly anhydrous dimethyl sulfoxide (DMSO) [55] and that such inactivity might be a direct result of protein solubilization in the organic milieu, which causes deleterious changes in the proteins secondary and tertiary structures [56]. However, different authors have recently reported that some proteases, namely thermolysin (from Bacillus thermo-proteolyticus) and Proleather (from Bacillus subtilis), were still active in pure DMSO, despite the fact that proteins were indeed solubilized. The former enzyme cata-... 

Antohi (34) has reported several possible isozyme structures of a malic acid decarboxylating enzyme in Bacillus subtilis, and Peak (35) has reported the same in Euglena gracilis this must be kept in mind for the Leuconostoc oenos system. It is possible that the enzymatic activities that we have reported (6,7,8) may be the result of isozyme interactions of the same protein. 

There are other types of transcriptional activators in bacteria. One is transcription factor 1 (TF1) encoded by a Bacillus subtilis phage. It is a member of the protein HU family (Chapter 27). However, unlike the nonspecific HU it binds to some sites specifically and activates transcription.143 The E. coli Ada protein is the acceptor protein in removal of methyl groups from DNA (Chapter 27). The same protein is an inducer of transcription of DNA repair enzymes in the large ada regulon. Methylation of Cys 69 of the Ada protein itself converts it into a gene activator.144... 

In the absence of 02 the E. coli FNR protein induces proteins of the anaerobic respiration pathways. Nitrate also has its own two-component system that senses nitrate availability and activates transcription of enzymes catalyzing nitrate respiration.162 An expanded two-component system induces sporulation in Bacillus subtilis in response to poor growth conditions.163164 The crystal structure of one of two response regulators (SpoOF) has a structure closely related to that of CheY and the nitrate response regulator NarL. 

The same enzyme has been highly purified from another strain (strain K) of Bacillus subtilis, and their properties have been fully investigated by Yamasaki and Arima (119, 120). They have confirmed the findings by Nishimura and Maruo and have found, moreover, that ATP and dATP strongly inhibit the enzyme. Yamasaki and Arima suggested that ATP might participate in the regulation of intracellular RNase activity. 

In 1964, Anraku (2, S) reported the isolation of an enzyme from Escherichia coli B which hydrolyzed ribonudeoside 2, 3 -cyclic phosphates. Enzyme fractions representing a 900-fold purification also possessed 3 -nucleotidase activity. Similar activities have subsequently been purified from Proteus mirabilis (4, 5), halophilic Vibrio algino-lyticus (6, 7), Bacillus subtilis (8), and various Enterobacteriaceae, specifically, Shigella sonnei, Salmonella heidelberg, Serratia marcescens, Proteus vulgaris (9), and others (10). The enzyme from each organism is strikingly similar, but some differences are apparent. 

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