Alignment of the predicted black cohosh CAS1 with cycloartenol synthase in Panax ginseng (OSCPNX1). The sequence consensus (Cons) of the alignment including residues with functionally similar side groups (indicated by “+”) is shown between the CAS1 and OSCPNX1 sequences. Amino acids marked by asterisks are highly conserved residues forming the squalene cyclase active site cavity in oxidosqualene cyclases (pfam pattern cd02892: SQCY_1); the catalytic aspartate required for protonation of the first C=C double-bond in squalene is boxed, as are the multiple residues that correspond to the conserved terpene synthase signature pattern (Prosite pattern, PS01074) in both sequences. Filled triangles underneath the alignment indicate Tyr410, His477, and Ile481, which direct specificity of the product, cycloartenol, in CAS1 of A. thaliana (Phillips et al. 2006)
As can be seen in Fig. 3, CAS1 and OSCPNX1 had 80% identity
(91% similarity) and shared 33 out of 34 residues that are highly
conserved among OSCs and a conserved terpene synthase signature
The predicted CAS1 protein contained conserved residues and
signature motifs (Fig. 3) typical of oxidosqualene cyclases
and terpene synthases, and also conserved amino acids that
determine the CAS product specificity.
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