Bacillus subtilis substrate specificity

Andersen, R.B. Neuhard, J. Deoxynucleoside kinases encoded by the yaaC and yaaF genes of Bacillus subtilis. Substrate specificity and kinetic analysis of deoxyguanosine kinase with UTP as the preferred phosphate donor. J. Biol. Chem., 276, 5518-5524 (2001)... 

Singh, S.K. Matsuno, K. LaPorte, D.C. Banaszak, L.J. Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase. J. Biol. Chem., 276, 26154-26163 (2001)... 

Thermolysin belongs to a class of proteases (called neutral proteases) which are distinct from the serine proteases, sulfhydryl proteases, metal-loexopeptidases, and acid proteases. Neutral proteases A and B from Bacillus subtilis resemble thermolysin in molecular weight, substrate specificity, amino acid content, and metal ion dependence. Since physiological substrates are most likely proteins, it is difficult to design simple experiments that can be interpreted in terms of substrate specificity and relative velocities. Therefore, studies of substrate specificity and other kinetic parameters must be carried out on di- and tripeptides so that details of the mechanism of catalysis can be obtained and interpreted simply. 

Lentz, O., Urlacher, V., and Schmid, R. D. 2004 Substrate specificity of native and mutated cytochrome P450 (CYP102A3) from Bacillus subtilis. J. Biotechnol., 108, 41-A9. 

Krispin, O., Alhnansbeiger, R. (1998). The Bacillus subtilis AraE protein displays a broad substrate specificity for several substrates. Journal of Bacteriology, 180, 3250 3252. 

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... 

The substrate specifity of Bacillus subtilis amylase was studied by Robyt and French (11) by using maltodextrins as well. These authors employed, among others, maltooctaose as a substrate for the investigation of Bacillus polymixa... 

It is noteworthy that nonribosomal peptide synthetase is similarly posttrans-lationally modified by covalent attachment of the 4 -phosphopantetheine group to the peptidyl carrier protein (PCP) [193-198]. While the ACPS can modify various apo-ACPs [167,173,187-189,191,192],it failed to modify PCPs from a variety of peptide synthetases [189]. This led to the discovery of the second family of PPTases [189], such as EntD from E. coli [189, 199, 200], Sfp from Bacillus subtilis [189,200-204], PptT from M. tuberculosis [264], and Gsp from B. brevis [ 189,205,206], required for the biosynthesis of enterobactin, surfactin, mycobactin, and gramicidin S, respectively. In contrast to ACPS, proteins in the latter family, such as Sfp, showed broader substrate specificity, modifying apo-PCPs, apo-ACPs, as well as apo-aryl carrier proteins and utilizing both CoA, acyl CoAs, and CoA analogs [204]. 

Gupta, N. and Farinas, E.T. (2010) Directed evolution of CotA laccase for increased substrate specificity using Bacillus subtilis spores. Protein Eng. Des. Sel, 23, 679-682. 

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