Isoprenoid in the context of "Salvia divinorum"

The Purple Earth hypothesis (PEH) is an astrobiological hypothesis, first proposed by molecular biologist Shiladitya DasSarma in 2007, that the earliest photosynthetic life forms of Early Earth were based on the simpler molecule retinal rather than the more complex porphyrin-based chlorophyll, making the surface biosphere appear purplish rather than its current greenish color. It is estimated to have occurred between 3.5 and 2.4 billion years ago during the Archean eon, prior to the Great Oxygenation Event and Huronian glaciation.

Retinal-containing cell membranes exhibit a single light absorption peak centered in the energy-rich green-yellow region of the visible spectrum, but transmit and reflect red and blue light, resulting in a magenta color. Chlorophyll pigments, in contrast, absorb red and blue light, but little or no green light, which results in the characteristic green reflection of plants, cyanobacteria, green algae, and other organisms with chlorophyllic organelles. The simplicity of retinal pigments in comparison to the more complex chlorophyll, their association with isoprenoid lipids in the cell membrane, as well as the discovery of archaeal membrane components in ancient sediments on the Early Earth are consistent with an early appearance of life forms with purple membranes prior to the turquoise of the Canfield ocean and later green photosynthetic organisms.

A peroxisome (/pəˈrɒksɪˌsoʊm/) is a membrane-bound organelle, a type of microbody, found in the cytoplasm of virtually all eukaryotic cells. Peroxisomes are oxidative organelles. Frequently, molecular oxygen serves as a co-substrate, from which hydrogen peroxide (H₂O₂) is then formed. Peroxisomes owe their name to hydrogen peroxide-generating and scavenging activities. They perform key roles in lipid metabolism and the reduction of reactive oxygen species.

Peroxisomes are involved in the catabolism of very long chain fatty acids, branched chain fatty acids, bile acid intermediates (in the liver), D-amino acids, and polyamines. Peroxisomes also play a role in the biosynthesis of plasmalogens: ether phospholipids critical for the normal function of mammalian brains and lungs. Peroxisomes contain approximately 10% of the total activity of two enzymes (Glucose-6-phosphate dehydrogenase and 6-Phosphogluconate dehydrogenase) in the pentose phosphate pathway, which is important for energy metabolism. It is debated whether peroxisomes are involved in isoprenoid and cholesterol synthesis in animals. Other peroxisomal functions include the glyoxylate cycle in germinating seeds ("glyoxysomes"), photorespiration in leaves, glycolysis in trypanosomes ("glycosomes"), and methanol and amine oxidation and assimilation in some yeasts.

An apicoplast is a derived non-photosynthetic plastid found in most Apicomplexa, including Toxoplasma gondii, and Plasmodium falciparum and other Plasmodium spp. (parasites causing malaria), but not in others such as Cryptosporidium. It originated from algae through secondary endosymbiosis; there is debate as to whether this was a green or red alga. The apicoplast is surrounded by four membranes within the outermost part of the endomembrane system. The apicoplast hosts important metabolic pathways like fatty acid synthesis, isoprenoid precursor synthesis and parts of the heme biosynthetic pathway.

Tocotrienols are plant-derived natural products belonging to the vitamin E family of diterpenoids. They exist as four isomers (alpha, beta, gamma, delta), each differing in the number and position of methyl groups on their chromanol ring. Tocotrienols are distinguished from the closely related tocopherols by their side chains: tocotrienols have three unsaturated isoprenoid double bonds, whereas tocopherols have a fully saturated side chain.

Tocotrienols are compounds naturally occurring in some foods sources, the richest being palm oil, but to a lesser extent rice bran oil, barley, oats, and certain seeds, nuts and grains, and the oils derived from them.

Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:

This enzyme participates in the pentose phosphate pathway (see image), a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the reduced form of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). The NADPH in turn maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage from compounds like hydrogen peroxide. Of greater quantitative importance is the production of NADPH for tissues involved in biosynthesis of fatty acids or isoprenoids, such as the liver, mammary glands, adipose tissue, and the adrenal glands. G6PD reduces NADP to NADPH while oxidizing glucose-6-phosphate. Glucose-6-phosphate dehydrogenase is also an enzyme in the Entner–Doudoroff pathway, a type of glycolysis.