Ontology highlight
ABSTRACT:
SUBMITTER: Aaron JA
PROVIDER: S-EPMC3090183 | biostudies-literature | 2010
REPOSITORIES: biostudies-literature
Pure and applied chemistry. Chimie pure et appliquee 20100101 8
Terpenoid synthases are ubiquitous enzymes that catalyze the formation of structurally and stereochemically diverse isoprenoid natural products. Many isoprenoid coupling enzymes and terpenoid cyclases from bacteria, fungi, protists, plants, and animals share the class I terpenoid synthase fold. Despite generally low amino acid sequence identity among these examples, class I terpenoid synthases contain conserved metal binding motifs that coordinate to a trinuclear metal cluster. This cluster not ...[more]