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A biosynthetic 3-hydroxy-3-methylglutaryl coenzyme A reductase (EC1.1.1.34 ), the rate-limiting enzyme of the mevalonate pathway for isopentenyl diphosphate biosynthesis, had previously been purified fromStreptomyces sp. strain CL190 and its corresponding gene (hmgr ) had been cloned (S. Takahashi, T. Kuzuyama, and H. Seto, J. Bacteriol. 181:1256–1263, 1999). Sequence analysis of the flanking regions of thehmgr gene revealed five new open reading frames,orfA to -E , which showed similarity to those encoding eucaryotic and archaebacterial enzymes for the mevalonate pathway. Feeding experiments with [1-13 C]acetate demonstrated thatEscherichia coli JM109 harboring thehmgr gene and these open reading frames used the mevalonate pathway under induction with isopropyl β-d -thiogalactopyranoside. This transformant could grow in the presence of fosmidomycin, a potent and specific inhibitor of the nonmevalonate pathway, indicating that the mevalonate pathway, intrinsically absent inE. coli , is operating in theE. coli transformant. Thehmgr gene andorfABCDE are thus unambiguously shown to be responsible for the mevalonate pathway and to form a gene cluster in the genome ofStreptomyces sp. strain CL190.

A Gene Cluster for the Mevalonate Pathway from Streptomyces sp. Strain CL190