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- Title
Poly(silicate)-metabolizing silicatein in siliceous spicules and silicasomes of demosponges comprises dual enzymatic activities (silica polymerase and silica esterase).
- Authors
Müller, Werner E. G.; Schloßmacher, Ute; Xiaohong Wang; Boreiko, Alexandra; Brandt, David; Wolf, Stephan E.; Tremel, Wolfgang; Schröder, Heinz C.
- 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.
- Subjects
SPONGES (Invertebrates); SPICULE (Anatomy); SILICA; SILICATES; ORGANELLES; ENZYMES; POLYMERIZATION; POLYCONDENSATION
- Publication
FEBS Journal, 2008, Vol 275, Issue 2, p362
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2007.06206.x