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In enzymology, a NADPH dehydrogenase is an enzyme that catalyzes In enzymology, a NAD (P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction NAD (P)H + H+ + a quinone↔ NAD (P)+ + a hydroquinone. The 4 substrates of this enzyme are NADH, NADPH, H+, and quinone, whereas its 3 products are NAD+, NADP+, and hydroquinone.http://www.creative-enzymes.com/product/Native-Bacillus-Megaterium-Diaphorase-NADH-_738.html
Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides, and plays an important role in cellular energy homeostasis.http://www.creative-enzymes.com/product/Native-Bacillus-Stearothermophilus-Myokinase_1306.html
Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase.http://www.creative-enzymes.com/product/Native-Escherichia-Coli-Alkaline-Phosphatase_1361.html
Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) assist in the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose and hemicellulose, in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds.http://www.creative-enzymes.com/product/Native-Microorganism-Glucosidase-MALTASE-_790.html
In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction: creatine + H2O ↔sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. The native enzyme was shown to be made up of two subunit monomers via SDS-polyacrylamide gel electrophoresis. Creatinase has been found to be most active at pH 8 and is most stable between ph 6-8 for 24 hrs. at 37 degrees. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. This enzyme participates in arginine and proline metabolism.http://www.creative-enzymes.com/product/Native-Microorganism-Creatine-Amidohydrolase_781.html
A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.http://www.creative-enzymes.com/product/Native-Microorganism-Dlactate-Dehydrogenase_803.html
Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels.http://www.creative-enzymes.com/product/Native-Porcine-Angiotensin-Converting-Enzyme_968.html
Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). 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.http://www.creative-enzymes.com/product/Native-Porcine-GlutamicPyruvic-Transaminase_1198.html
The Long chain fatty acyl-CoA synthetase enzyme is a member of the ligase family that activates the breakdown of complex fatty acids. Long chain fatty acyl-CoA synthetase plays a crucial role in intermediary metabolism by catalyzing the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. It is an enzyme present in all organisms from bacteria to humans. It catalyzes the pre-step reaction for β-oxidation of fatty acids or can be incorporated in phospholipids.http://www.creative-enzymes.com/product/Native-Pseudomonas-Fragi-AcylCoA-Synthetase_1685.html
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