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.
Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.
In enzymology, an erythrose-4-phosphate dehydrogenase (EC 1.2.1.72) is an enzyme that catalyzes the chemical reaction
In enzymology, a homoserine dehydrogenase (EC 1.1.1.3) is an enzyme that catalyzes the chemical reaction
In enzymology, histidinol dehydrogenase (HIS4) (HDH) (EC 1.1.1.23) is an enzyme that catalyzes the chemical reaction
In enzymology, a homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction
In enzymology, a 4-phosphoerythronate dehydogenase (EC 1.1.1.290) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-threonine 3-dehydrogenase (EC 1.1.1.103) is an enzyme that catalyzes the chemical reaction
In enzymology, a pyridoxal 4-dehydrogenase (EC 1.1.1.107) is an enzyme that catalyzes the chemical reaction
In enzymology, a glycerol-3-phosphate dehydrogenase [NAD(P)+] (EC 1.1.1.94) is an enzyme that catalyzes the chemical reaction
In enzymology, an aspartate-semialdehyde dehydrogenase is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it.
In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction
In enzymology, a glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) is an enzyme that catalyzes the chemical reaction
In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) is an enzyme that catalyzes the chemical reaction
Aspartate dehydrogenase (EC 1.4.1.21) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-amino-acid dehydrogenase (EC 1.4.1.5) 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
In enzymology, a saccharopine dehydrogenase (NAD+, L-lysine-forming) (EC 1.5.1.7) is an enzyme that catalyzes the chemical reaction
In enzymology, a pyridoxine 5'-phosphate synthase (EC 2.6.99.2) is an enzyme that catalyzes the chemical reaction
Phosphoserine transaminase is an enzyme with systematic name O-phospho-L-serine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction
