Purification, kinetics, inhibitors and CD for recombinant β-amyrin synthase fromEuphorbia tirucalli L and functional analysis of the DCTA motif, which is highly conserved among oxidosqualene cyclases

Ryousuke Ito, Yukari Masukawa, Tsutomu Hoshino
  • FEBS Journal, February 2013, Wiley
  • DOI: 10.1111/febs.12119

Characterization of beta-amyrin synthase from Euphorbia tirucalli

What is it about?

Expression of beta-amyrin synthase in Saccharomyces cerevisiae lacking lanosterol synthase. Km and kcat values are reported. Ki values of a few inhibitors are determined. Proton donor to initiate the polycyclization reaction is determined by the site-directed mutagenesis.

Why is it important?

Complete purification of oxidosqualene cyclases has not been reported except for human lanosterol synthase. This is the second paper for the complete purification. Thus, we could report the detailed enzymatic characterization of beta-amyrin synthase.

Perspectives

Tsutomu Hoshino
Niigata University

This paper can help the researchers, who have engaged in the studies on oxidosqualene synthases, to identify the active site residues and their functions.

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http://dx.doi.org/10.1111/febs.12119

The following have contributed to this page: Tsutomu Hoshino

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