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.
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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
This paper can help the researchers, who have engaged in the studies on oxidosqualene synthases, to identify the active site residues and their functions.
Tsutomu Hoshino
Niigata University
Read the Original
This page is a summary of: Purification, kinetics, inhibitors and CD for recombinant β‐amyrin synthase from Euphorbia tirucalli L and functional analysis of the DCTA motif, which is highly conserved among oxidosqualene cyclases, FEBS Journal, February 2013, Wiley,
DOI: 10.1111/febs.12119.
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