期刊
PURE AND APPLIED CHEMISTRY
卷 82, 期 8, 页码 1585-1597出版社
WALTER DE GRUYTER GMBH
DOI: 10.1351/PAC-CON-09-09-37
关键词
enzyme catalysis; farnesyl diphosphate; geranyl diphosphate; inorganic pyrophosphate; Mg2+
资金
- NIGMS NIH HHS [R01 GM056838-14, R01 GM056838] Funding Source: Medline
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 only serves to bind and orient the flexible isoprenoid substrate in the precatalytic Michaelis complex, but it also triggers the departure of the diphosphate leaving group to generate a carbocation that initiates catalysis. Additional conserved hydrogen bond donors assist the metal cluster in this function. Crystal structure analysis reveals that the constellation of three metal ions required for terpenoid synthase catalysis is generally identical among all class I terpenoid synthases of known structure.
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