What is it about?

A synthetic pathway of sialic acid found in bacteria is different from that in mammalian cells, which provides a new target for anti-meningitis drug.

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Why is it important?

This is a good example that in vitro study of an enzyme doesn't represent its in vivo function. Although CMP-NeuAc synthetase NeuA, a bi-function enzyme found in E. coli and Streptococcus suis, was able to catalyze formation of CMP-NeuAc in vitro, we found that this enzyme only catalyze the synthesis of CMP-O-acetyl-NeuAc in vivo. Therefore, the true pathway of sialic acid activation in vivo is O-acetylation of NeuAc, activation of O-acetyl-NeuAc, and then de-acetylation to form CMP-NeuAc.

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This page is a summary of: NeuA O-acetylesterase activity is specific for CMP-activated O-acetyl sialic acid in Streptococcus suis serotype 2, Biochemical and Biophysical Research Communications, July 2011, Elsevier,
DOI: 10.1016/j.bbrc.2011.05.092.
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