NDLI: d biochemical characterization of mirror image barnase †

Content Provider	Semantic Scholar
Author	Vinogradov, Alexander A. Evans, Ethan D. Pentelute, Bradley L.
Copyright Year	2015
Abstract	In this study we synthesized and characterizedmirror image barnase (B. amyloliqiens ribonuclease). DBarnase was identical to L-barnase, when analyzed by liquid chromatography and mass-spectrometry. Proteolysis of the mirror image enzyme revealed that in contrast to its native counterpart, D-barnase was completely stable to digestive proteases. In enzymatic assays, D-barnase had the reciprocal chiral specificity and was fully active towards mirror image substrates. Interestingly, D-barnase also hydrolyzed the substrate of the native chirality, albeit 4000 times less efficiently. This effect was further confirmed by digesting a native 112-mer RNA with the enzyme. Additional studies revealed that barnase accommodates a range of substrates with various chiralities, but the prime requirement for guanosine remains. These studies point toward using mirror image enzymes as modern agents in biotechnology.
File Format	PDF HTM / HTML
Alternate Webpage(s)	https://pubs.rsc.org/en/Content/ArticlePDF/2015/SC/C4SC03877K
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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