Differences in HDR product preference present a novel mechanism in plants to control substrate availability for short- and long-chain isoprenoids.

Malaria parasites target a polyprenyl synthase enzyme to the apicoplast organelle and require its activity to produce long-chain linear isoprenoids necessary for apicoplast biogenesis.

It is hypothesized that volatile organic compounds emitted by plants after stress induction may be sensed by neighboring eavesdropping plants using odorant-binding proteins.

Type 1 polyisoprenoid diphosphate phosphatase (PDP1) contributes to interconversion of isoprenols and isoprenylpyrophosphates, balancing the sterol and nonsterol branches of the mevalonate pathway by regulating ERAD of HMG CoA reductase and ER-to-Golgi transport of UBIAD1.

A combination of phylogenetic and biochemical analyses suggest that some unexpected variations in the synthesis of isoprenoids may be widespread across all three domains of life.

The inhibition of sterol-accelerated degradation of HMG CoA reductase by the vitamin K2 synthetic enzyme UBIAD1 may contribute to the accumulation of cholesterol that is associated with Schnyder corneal dystrophy.

Mutations in four members of the mevalonate pathway have been identified from 134 index porokeratosis patients, including some that correlate with specific clinical manifestations of the disease.

UBIAD1 mediates a unique geranylgeranyl pyrophosphate-sensing mechanism that when disrupted, inhibits degradation of HMG CoA reductase and triggers overproduction of corneal cholesterol that characterizes the eye disease Schnyder Corneal Dystrophy.

The pyruvate kinase contained in the apicoplast organelle of malaria parasites makes the nucleotide triphosphates required for several processes including transcription of the organellar genome.

Combined cutting-edge technologies discovered a pair of carboxylate transporters that appears evolutionarily different among novel transporters and that is essential for parasite physiology.