Bacillus subtilis extracellular

Hirose I et al. Proteome analysis of Bacillus subtilis extracellular proteins a two-dimensional protein electrophoretic study. Microbiology 2000 146 65-75. 

Corvey, C. et al (2003) Activation of subtilin precursors by Bacillus subtilis extracellular serine proteases subtil-isin (AprE), WprA, and Vpr. Biachem. Biaphys. Res. Cammun., 304 (1), 48 - 54. 

Structural analysis of the two pectate lyases PelC and PelE (5, 6), demonstrated that these proteins fold in a large heHx of parallel P strands. A stack of asparagine residues parallel to the helix probably plays a role in the stabUity of this structure. Identification of the structurally conserved amino adds lead to a reaHgnment of the protein sequences (7). In addition to Erwinia extracellular pectate lyases, the multiple aHgnment indudes the Bacillus subtilis pectate lyase, Aspergillus tdger and E. carotovora pectin lyases and plant proteins. 

Wu, X.C., Lee, W., Tran, L. and Wong, S.L. (1991) Engineering a Bacillus subtilis expression-secretion system with a strain deficient in six extracellular proteases. Journal of Bacteriology, 173 (16), 4952 1958. 

Tanaka, T. Kawata, M. Gloning and characterization of Bacillus subtilis iep, which has positive and negative effects on production of extracellular proteases. J. Bacteriol., 170, 3593-3600 (1988)... 

An extracellular RNase of Bacillus subtilis strain H was isolated in crystalline state and its chemical nature studied by Nishimura and coworkers (112). It has a very complicated base specificity (113, 114)-However, with a few exceptions, the phosphodiester bonds of 3 -purine nucleotides are cleaved faster than those of 3 -pyrimidine nucleotides, and those of 3 -nucleotides with 6(4)-keto group are cleaved faster than those of 3 -nucleotides with a 6(4)-amino group. Thus, when adjacent bonds are the same, the following results ... 

Nishimura and Maruo (118) extracted and RNase from cells of Bacillus subtilis strain H, which is quite different from the extracellular RNases of the same strain. It is remarkable that the digestion products of RNA by the enzyme are exclusively four nucleoside 2, 3 -cyclic phosphates. 

Some bacterial species, such as Bacillus subtilis, have a genetically specified system that will allow them to take up extracellular DNA. Expression of the genes that make up this competence system (the... 

Solomon JM, Lazazzera BA, Grossman AD. Purification and characterization of an extracellular peptide factor that affects two different developmental pathways in Bacillus subtilis. Genes Dev. 1996 10 2014-2024. 

D-Galactanases have been reported to be produced by Bacillus subtilis, by a rumen anaerobic bacterium, by fungi, and by plants (see Table V). D-Galactanases are inductive, and those of microbial origin are usually produced extracellularly in response to the carbon source of the culture medium. 

In Abramowicz DA (ed). Biocatalysis. Van Nostrand Reinhold, New York, pp 277-318 Nasser W, Chalet F, Robert-Baudouy J (1990) Purification and characterization of extracellular pectate lyase from Bacillus subtilis. Biochimie 72(9) 689-695 Neidleman SL (1991) Historical perspective on the industrial uses of biocattilysts. In Dordick JS (ed). Biocatalysts for industry. Plenum Press, New York, pp 21-33 Neuhaus W, Novalin S, Klimacek, M et al. (2006) Optimization of an innovative hoUow-fiber process to produce lactose-reduced skim milk. Appl Biochem Biotechnol 134(1) 1-14 Nield BS, Willows RD, Torda AE et al. (2002) New enzymes from environmental cassette arrays functional attributes of a phosphotransferase and an RNA-methyltransferase. Protein Sci 13 1651-1659... 

Pottathil, M. and Lazazzera, BA. (2003). The extracellular phr Peptide-rap phosphatase signaling circuit o bacillus subtilis. Front Biosci. 1, 8 D32-45. 

Extracellular a-amylase was purified to homogeneity from Marburg strain of Bacillus subtilis. The enzyme is a single polypeptide chain of molecular weight approximately 67 000. Its A -terminal amino-acid sequence is (15). 

Kakeshita, H. et al (2010) Enhanced extracellular production of heterologous proteins in Bacillus subtilis by deleting the C-terminal region of the SecA secretory machinery. Mol Biotechnol, 46 (3), 250- 257. 

Veening, J.W. et al (2008) Transient heterogeneity in extracellular protease production by Bacillus subtilis. Mol. Syst Biol, 4, 184. 

Antelmann, H. et al. (2003) The extracellular proteome of Bacillus subtilis under secretion stress conditions. Mol Microbiol, 49 (1), 143-156. 

Szczesna-Antczak M, Antczak T, Bielecki S (2004) Stability of extracellular proteinases productivity by Bacillus subtilis cells inunobilized in PVA-cryogel. Enzyme Microb Technol 34 168-176... 

Subtilisin (EC 3.4.21.4) an extracellular, single chain, alkaline serine protease from Bacillus subtilis and related species. S. are known from four different species of Bacillus S. Carlsberg (274 amino acid residues, M, 27,277), S. BPN (275 amino acid residues, M, 27,537), S. Novo (identical with S.BPN ) and S. amylosacchariticus (275 amino acid residues, M, 27671). The observed sequence differences between different S. represent conservative substitutions and are limited to the surface amino acids. Like the pancreatic proteinases, S. has catalytic Ser22i, His64 and Asnjj residues, but it is structurally very different from the other serine proteases, e. g. the active center of S. is -Thr-Ser-Met-, whereas that of the pancreatic enzymes is -Asp-Ser-Gly- pancreatic enzymes contain 4- disulfide bridges, whereas S. contains none S. contains 31 % a-helical structure and 3 spatially separated domains, whereas the pancreatic enzymes have 10-20% a-helical structure and a high content of p-structures in both types, the active center is a substrate cleft. S. also have a broader substrate specificity than the pancreatic enzymes. This is a notable example of the convergent evolution of catalytic activity in two structurally completely different classes of proteins. S. is used in the structural elucidation... 

A wide variety of microorganisms also produce many kinds of surface-active lipoproteins or lipopeptides [63]. Mostly they exhibit the typical amphiphilic character and are generally extracellular. Representative of such surface-active lipopeptides is surfactin produced by Bacillus subtilis. It is composed of a heptapeptide cycle closed by a C14.15 P-hydroxy fatty acid that forms a lactone ring system (Fig. 15) [64]. This structure resembles those of iturins, another class of lipopeptides also produced by Bacillus subtilis [65]. 

Lesuisse, E., K. Schanck, and C. Colson. 1993. Purification and Preliminary Characterization of the Extracellular Lipase of Bacillus Subtilis 168, an Extremely Basic pH-Tolerant Enzyme. European Journal of Biochemistry 216 (1) 155-160. 

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