| Geranial dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.86 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Geranial dehydrogenase (EC 1.2.1.86, GaDH, geoB (gene)) is an enzyme with systematic name geranial:NAD+ oxidoreductase. [1] [2] This enzyme catalyses the following chemical reaction
Does not act on neral.
Nepetalactone is a name for multiple iridoid analog stereoisomers. Nepetalactones are produced by Nepeta cataria (catnip) and many other plants belonging to the genus Nepeta, in which they protect these plants from herbivorous insects by functioning as insect repellents. They are also produced by many aphids, in which they are sex pheromones. Nepetalactones are cat attractants, and cause the behavioral effects that catnip induces in domestic cats. However, they affect visibly only about two thirds of adult cats. They produce similar behavioral effects in many other felids, especially in lions and jaguars. In 1941, the research group of Samuel M. McElvain was the first to determine the structures of nepetalactones and several related compounds.
Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen), respectively.
Biological carbon fixation or сarbon assimilation is the process by which inorganic carbon is converted to organic compounds by living organisms. The compounds are then used to store energy and as structure for other biomolecules. Carbon is primarily fixed through photosynthesis, but some organisms use a process called chemosynthesis in the absence of sunlight.
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form of NADP+, the oxidized form. NADP+ is used by all forms of cellular life.
Malate dehydrogenase (EC 1.1.1.37) (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD+ to NADH. This reaction is part of many metabolic pathways, including the citric acid cycle. Other malate dehydrogenases, which have other EC numbers and catalyze other reactions oxidizing malate, have qualified names like malate dehydrogenase (NADP+).
Isocitrate dehydrogenase (NAD+) (EC 1.1.1.41, isocitric dehydrogenase, beta-ketoglutaric-isocitric carboxylase, isocitric acid dehydrogenase, NAD dependent isocitrate dehydrogenase, NAD isocitrate dehydrogenase, NAD-linked isocitrate dehydrogenase, NAD-specific isocitrate dehydrogenase, NAD isocitric dehydrogenase, isocitrate dehydrogenase (NAD), IDH (ambiguous), nicotinamide adenine dinucleotide isocitrate dehydrogenase) is an enzyme with systematic name isocitrate:NAD+ oxidoreductase (decarboxylating). This enzyme catalyses the following chemical reaction
In biochemistry, mixed acid fermentation is the metabolic process by which a six-carbon sugar is converted into a complex and variable mixture of acids. It is an anaerobic (non-oxygen-requiring) fermentation reaction that is common in bacteria. It is characteristic for members of the Enterobacteriaceae, a large family of Gram-negative bacteria that includes E. coli.
3β-Hydroxysteroid dehydrogenase/Δ5-4 isomerase (3β-HSD) is an enzyme that catalyzes the biosynthesis of the steroid progesterone from pregnenolone, 17α-hydroxyprogesterone from 17α-hydroxypregnenolone, and androstenedione from dehydroepiandrosterone (DHEA) in the adrenal gland. It is the only enzyme in the adrenal pathway of corticosteroid synthesis that is not a member of the cytochrome P450 family. It is also present in other steroid-producing tissues, including the ovary, testis and placenta. In humans, there are two 3β-HSD isozymes encoded by the HSD3B1 and HSD3B2 genes.
Glycerol-3-phosphate dehydrogenase (GPDH) is an enzyme that catalyzes the reversible redox conversion of dihydroxyacetone phosphate to sn-glycerol 3-phosphate.
In enzymology, a geraniol dehydrogenase (EC 1.1.1.183) is an enzyme that catalyzes the chemical reaction
Glycerol dehydrogenase (EC 1.1.1.6, also known as NAD+-linked glycerol dehydrogenase, glycerol: NAD+ 2-oxidoreductase, GDH, GlDH, GlyDH) is an enzyme in the oxidoreductase family that utilizes the NAD+ to catalyze the oxidation of glycerol to form glycerone (dihydroxyacetone).
In enzymology, a methanol dehydrogenase (MDH) is an enzyme that catalyzes the chemical reaction:
In enzymology, a 7beta-hydroxysteroid dehydrogenase (NADP+) (EC 1.1.1.201) is an enzyme that catalyzes the chemical reaction
In enzymology, a methylmalonate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.27) is an enzyme that catalyzes the chemical reaction
In enzymology, a mycothiol-dependent formaldehyde dehydrogenase (EC 1.1.1.306) is an enzyme that catalyzes the chemical reaction
In enzymology, a NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction
Butyryl-coenzyme A is the coenzyme A-containing derivative of butyric acid. It is acted upon by butyryl-CoA dehydrogenase and an intermediary compound of ABE fermentation.
D-xylose reductase (EC 1.1.1.307, XylR, XyrA, msXR, dsXR, monospecific xylose reductase, dual specific xylose reductase, NAD(P)H-dependent xylose reductase, xylose reductase) is an enzyme with systematic name xylitol:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction
Quinate dehydrogenase (quinone) (EC 1.1.5.8, NAD(P)+-independent quinate dehydrogenase, quinate:pyrroloquinoline-quinone 5-oxidoreductase) is an enzyme with systematic name quinate:quinol 3-oxidoreductase. This enzyme catalyses the following chemical reaction
Valine dehydrogenase (NAD+) (EC 1.4.1.23) is an enzyme with systematic name L-valine:NAD+ oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction
