Poly(silicate)-metabolizing silicatein in siliceous spicules and silicasomes of demosponges comprises dual enzymatic activities (silica polymerase and silica esterase). Müller, W., E., G., Wolf, S., E., Schlossmacher, U., Wang, X., Boreiko, A., Brandt, D., Tremel, W., & Schröder, H. FEBS J., 275(2):362-70, 2008. Paper Website abstract bibtex Siliceous sponges can synthesize poly(silicate) for their spicules enzymatically using silicatein. We found that silicatein exists in silica-filled cell organelles (silicasomes) that transport the enzyme to the spicules. We show for the first time that recombinant silicatein acts as a silica polymerase and also as a silica esterase. The enzymatic polymerization/polycondensation of silicic acid follows a distinct course. In addition, we show that silicatein cleaves the ester-like bond in bis(p-aminophenoxy)-dimethylsilane. Enzymatic parameters for silica esterase activity are given. The reaction is completely blocked by sodium hexafluorosilicate and E-64. We consider that the dual function of silicatein (silica polymerase and silica esterase) will be useful for the rational synthesis of structured new silica biomaterials.
@article{
title = {Poly(silicate)-metabolizing silicatein in siliceous spicules and silicasomes of demosponges comprises dual enzymatic activities (silica polymerase and silica esterase).},
type = {article},
year = {2008},
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keywords = {Animals,Catalysis,Cathepsins,Cathepsins: metabolism,Electron,Enzymes,Enzymes: metabolism,Mass,Matrix-Assisted Laser Desorpti,Microscopy,Organelles,Organelles: enzymology,Organelles: metabolism,Porifera,Porifera: enzymology,Porifera: metabolism,Scanning,Silicates,Silicates: metabolism,Spectrometry},
pages = {362-70},
volume = {275},
websites = {http://www.ncbi.nlm.nih.gov/pubmed/18081864},
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abstract = {Siliceous sponges can synthesize poly(silicate) for their spicules enzymatically using silicatein. We found that silicatein exists in silica-filled cell organelles (silicasomes) that transport the enzyme to the spicules. We show for the first time that recombinant silicatein acts as a silica polymerase and also as a silica esterase. The enzymatic polymerization/polycondensation of silicic acid follows a distinct course. In addition, we show that silicatein cleaves the ester-like bond in bis(p-aminophenoxy)-dimethylsilane. Enzymatic parameters for silica esterase activity are given. The reaction is completely blocked by sodium hexafluorosilicate and E-64. We consider that the dual function of silicatein (silica polymerase and silica esterase) will be useful for the rational synthesis of structured new silica biomaterials.},
bibtype = {article},
author = {Müller, Werner E. G. and Wolf, Stephan E. and Schlossmacher, Ute and Wang, Xiao-Hong and Boreiko, Alexandra and Brandt, David and Tremel, Wolfgang and Schröder, Heinz-Christoph},
journal = {FEBS J.},
number = {2}
}
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