@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},
 identifiers = {[object Object]},
 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},
 id = {878e0fff-fc46-3c62-9be7-1c67f428c2f6},
 created = {2015-06-17T19:54:13.000Z},
 file_attached = {true},
 profile_id = {7ea5179c-6164-3904-ba32-9f8c1596df3b},
 last_modified = {2017-03-10T02:43:54.273Z},
 read = {true},
 starred = {false},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 citation_key = {Muller2008},
 private_publication = {false},
 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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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. 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