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Native Streptomyces sp. Phospholipase D LAB GRADE

Phospholipase D (PLD) is glycerophospholipid-specific. It is markedly less active on sphingomyelins and lysophospholipids. Phospholipase D hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid.

Native Arthrobacter sp. Tyramine Oxidase LAB GRADE

Amine oxidases (AO) are enzymes that catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing (EC and copper-containing (EC Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: RCH2NH2 + H2O + O2 ↔ RCHO + NH3 + H2O2. The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2.

Native Arthrobacter sp. acyl-CoA oxidase LAB GRADE

In enzymology, an acyl-CoA oxidase (EC is an enzyme that catalyzes the chemical reaction acyl-CoA + O2↔ trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD.


Native Bacillus sp. Glutamine synthetase LAB GRADE

Glutamine synthetase (GS) (EC is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine: Glutamate + ATP + NH3 → Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites.

Native Bovine Glutamate Dehydrogenase LAB GRADE 97%

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.

Native Cucurbita sp. L-ascorbate oxidase LAB GRADE

In enzymology, a L-ascorbate oxidase (EC is an enzyme that catalyzes the chemical reaction2 L-ascorbate + O2 ↔ 2 dehydroascorbate + 2 H2O. Thus, the two substrates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O.

Native Human Alanine Aminotransferase LAB GRADE 97%

Alanine transaminase (ALT) is a transaminase enzyme (EC It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels.

Native Microbial ?-phosphoglucomutase LAB GRADE 97%

Phosphoglucomutase (EC is an enzyme that transfers a phosphate group on an α-D-glucose monomer from the 1' to the 6' position in the forward direction or the 6' to the 1' position in the reverse direction. More precisely, it facilitates the interconversion of glucose 1-phosphate and glucose 6-phosphate.

Native Microorganism Cholesterol Oxidase LAB GRADE

Recombinant Cholesterol Oxidase belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. This enzyme participates in bile acid biosynthesis.

Native Microorganism Pyruvate oxidase LAB GRADE 97%

In enzymology, a pyruvate oxidase (EC is an enzyme that catalyzes the chemical reaction: pyruvate + phosphate + O2 ↔ acetyl phosphate + CO2 + H2O2. The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.

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