| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5166805 | Phytochemistry | 2009 | 4 Pages |
Abstract
Functional analysis of a putative second terpene synthase (TPS) divalent metal binding motif is presented. Specifically, to probe the surprising observation that plant TPS occasionally contain Gly in place of an otherwise conserved Thr/Ser that has been observed to directly ligate a divalent metal ion.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Ke Zhou, Reuben J. Peters,