| Geraniol isomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.4.4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Geraniol isomerase (EC 5.4.4.4) is an enzyme with systematic name geraniol hydroxymutase. [1] [2] This enzyme catalyses the following chemical reaction
In absence of oxygen the bifunctional linalool dehydratase-isomerase could act as an enzyme from this class.
Enoyl-CoA-(∆) isomerase (EC 5.3.3.8, also known as dodecenoyl-CoA- isomerase, 3,2-trans-enoyl-CoA isomerase, ∆3 ,∆2 -enoyl-CoA isomerase, or acetylene-allene isomerase, is an enzyme that catalyzes the conversion of cis- or trans-double bonds of coenzyme A bound fatty acids at gamma-carbon to trans double bonds at beta-carbon as below:
Geraniol is a monoterpenoid and an alcohol. It is the primary component of citronella oil and is a primary component of rose oil, palmarosa oil. It is a colorless oil, although commercial samples can appear yellow. It has low solubility in water, but it is soluble in common organic solvents. The functional group derived from geraniol is called geranyl.
Linalool refers to two enantiomers of a naturally occurring terpene alcohol found in many flowers and spice plants. Linalool has multiple commercial applications, the majority of which are based on its pleasant scent. A colorless oil, linalool is classified as an acyclic monoterpenoid. In plants, it is a metabolite, a volatile oil component, an antimicrobial agent, and an aroma compound. Linalool has uses in manufacturing of soaps, fragrances, food additives as flavors, household products, and insecticides. Esters of linalool are referred to as linalyl, e.g. linalyl pyrophosphate, an isomer of geranyl pyrophosphate.
Glucose-6-phosphate isomerase (GPI), alternatively known as phosphoglucose isomerase/phosphoglucoisomerase (PGI) or phosphohexose isomerase (PHI), is an enzyme that in humans is encoded by the GPI gene on chromosome 19. This gene encodes a member of the glucose phosphate isomerase protein family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In the cytoplasm, the gene product functions as a glycolytic enzyme that interconverts glucose-6-phosphate (G6P) and fructose-6-phosphate (F6P). Extracellularly, the encoded protein functions as a neurotrophic factor that promotes survival of skeletal motor neurons and sensory neurons, and as a lymphokine that induces immunoglobulin secretion. The encoded protein is also referred to as autocrine motility factor (AMF) based on an additional function as a tumor-secreted cytokine and angiogenic factor. Defects in this gene are the cause of nonspherocytic hemolytic anemia, and a severe enzyme deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
Monoterpenes are a class of terpenes that consist of two isoprene units and have the molecular formula C10H16. Monoterpenes may be linear (acyclic) or contain rings (monocyclic and bicyclic). Modified terpenes, such as those containing oxygen functionality or missing a methyl group, are called monoterpenoids. Monoterpenes and monoterpenoids are diverse. They have relevance to the pharmaceutical, cosmetic, agricultural, and food industries.
6-Phosphogluconolactonase (EC 3.1.1.31, 6PGL, PGLS, systematic name 6-phospho-D-glucono-1,5-lactone lactonohydrolase) is a cytosolic enzyme found in all organisms that catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in the oxidative phase of the pentose phosphate pathway:
D-Xylose is a five-carbon aldose that can be catabolized or metabolized into useful products by a variety of organisms.
Aminolevulinic acid dehydratase (porphobilinogen synthase, or ALA dehydratase, or aminolevulinate dehydratase) is an enzyme (EC 4.2.1.24) that in humans is encoded by the ALAD gene. Porphobilinogen synthase (or ALA dehydratase, or aminolevulinate dehydratase) synthesizes porphobilinogen through the asymmetric condensation of two molecules of aminolevulinic acid. All natural tetrapyrroles, including hemes, chlorophylls and vitamin B12, share porphobilinogen as a common precursor. Porphobilinogen synthase is the prototype morpheein.
In enzymology, an ascopyrone tautomerase is an enzyme that catalyzes the chemical reaction
The enzyme hydroperoxide dehydratase (EC 4.2.1.92) catalyzes the chemical reaction
D-bifunctional protein (DBP), also known as peroxisomal multifunctional enzyme type 2 (MFP-2), as well as 17β-hydroxysteroid dehydrogenase type IV is a protein that in humans is encoded by the HSD17B4 gene. It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and steroid metabolism.
Pterin-4-alpha-carbinolamine dehydratase is an enzyme that in humans is encoded by the PCBD1 gene.
Geranial dehydrogenase (EC 1.2.1.86, GaDH, geoB (gene)) is an enzyme with systematic name geranial:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
Linoleate 8R-lipoxygenase (EC 1.13.11.60, linoleic acid 8R-dioxygenase, 5,8-LDS (bifunctional enzyme), 7,8-LDS (bifunctional enzyme), 5,8-linoleate diol synthase (bifunctional enzyme), 7,8-linoleate diol synthase (bifunctional enzyme), PpoA) is an enzyme with systematic name linoleate:oxygen (8R)-oxidoreductase. This enzyme catalyses the following chemical reaction
Geraniol 8-hydroxylase (EC 1.14.14.83, Formerly EC 1.14.13.152, CYP76B6, G10H, CrG10H, SmG10H) is an enzyme with systematic name geraniol,NADPH:oxygen oxidoreductase (8-hydroxylating). This enzyme catalyses the following chemical reaction
4-hydroxybutanoyl-CoA dehydratase (EC 4.2.1.120) is an enzyme with systematic name 4-hydroxybutanoyl-CoA hydro-lyase. This enzyme catalyses the following chemical reaction
Linalool dehydratase (EC 4.2.1.127, linalool hydro-lyase (myrcene-forming)) is an enzyme with systematic name (3S)-linalool hydro-lyase (myrcene-forming). This enzyme catalyses the following chemical reaction
6-phospho-3-hexuloisomerase is an enzyme with systematic name D-arabino-hex-3-ulose-6-phosphate isomerase. This enzyme catalyses the following chemical reaction
9,12-octadecadienoate 8-hydroperoxide 8R-isomerase is an enzyme with systematic name (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate hydroxymutase ( -5,8-dihydroxyoctadeca-9,12-dienoate-forming). This enzyme catalyses the following chemical reaction
Thauera linaloolentis is a gram-negative, mesophilic, motile bacterium from the genus of Thauera.
