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Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate.http://www.creative-enzymes.com/product/Native-Microorganism-Glutamate-Dehydrogenase-NADdependent-_793.html
In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle).http://www.creative-enzymes.com/product/Native-Pseudomonas-Lemoignei-Hydroxybutyrate-Dehydrogenase_1072.html
In enzymology, a 3alpha-hydroxysteroid dehydrogenase (B-specific) (EC 1.1.1.50) is an enzyme that catalyzes the chemical reaction:androsterone + NAD (P)+↔ 5alpha-androstane-3,17-dione + NAD (P)H + H+. The 3 substRates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor, more specifically it is part of the group of hydroxysteroid dehydrogenases.http://www.creative-enzymes.com/product/Native-Pseudomonas-Testosteroni-3-Hydroxysteroid-Dehydrogenase_1014.html
http://www.creative-enzymes.com/product/3AcetylpyridineAdenine-Dinucleotide-Phosphate-Oxidized-APADP-_1509.html
In enzymology, a glycerophosphocholine phosphodiesterase (EC 3.1.4.2) is an enzyme that catalyzes the chemical reaction: sn-glycero-3-phosphocholine + H2O↔ choline + sn-glycerol 3-phosphate. Thus, the two substrates of this enzyme are sn-glycero-3-phosphocholine and H2O, whereas its two products are choline and sn-glycerol 3-phosphate.http://www.creative-enzymes.com/product/Native-Gliocladium-Roseum-Glycerophosphocholine-Phosphodiesterase_749.html
Acetyl-coenzyme A synthetase catalyzes the production of acetyl-CoA. It is involved in histone acetylation in the nucleus. It may be involved in the growth of nonfermentable carbon sources such as glycerol. Acetyl-coenzyme A synthetase is induced by acetate, acetaldehyde and ethanol.http://www.creative-enzymes.com/product/Native-Bakers-Yeast-S-Cerevisiae-SAcetylcoenzyme-A-Synthetase_1439.html
Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides.http://www.creative-enzymes.com/product/Native-Electrophorus-Electricus-electric-Eel-Acetylcholinesterase_920.html
In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle).http://www.creative-enzymes.com/product/Native-Rhodopseudomonas-Sphaeroides-Hydroxybutyrate-Dehydrogenase_1073.html
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