Silicateins are a class of biomineralizing enzymes (~23–27 kDa in their active form) that catalyze and template silica mineralization while directing skeletal growth in a variety of marine sponges. They share a close evolutionary relationship with a well-characterized family of proteolytic digestive enzymes, but are distinguished by unique self-assembling and mineralizing functionalities. Silicateins were first discovered as the majority protein fraction occluded within needle-like biosilica skeletal elements of the marine sponge Tethya aurantia (Shimizu et al. 1998; Weaver and Morse 2003), and were later identified in a number of other siliceous sponge species as well (Wang et al. 2012; Schröder et al. 2007). Research elucidating silicatein structure and function has provided insights into the molecular mechanisms of natural silica...
- Bawazer LA et al (2012) Evolutionary selection of enzymatically synthesized semiconductors from biomimetic mineralization vesicles. Proc Natl Acad Sci. Accepted (in press)Google Scholar