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Native Proteus sp. Glutamate Dehydrogenase (NADP-dependent) LAB GRADE

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-Proteus-Sp-Glutamate-Dehydrogenase-NADPdependent-_792.html
 

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Native Proteus sp. Glutamate Dehydrogenase (NADP-dependent) 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.http://www.creative-enzymes.com/product/Native-Proteus-Sp-Glutamate-Dehydrogenase-NADPdependent-_792.html

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Native Pseudomonas atlantica Agarase LAB GRADE 97%

Agarase is an enzyme with system name agarose 4-glycanohydrolase. It found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of Carbon and enables their ability to thrive in the ocean. Agarases are classified as either α-agarases or β-agarases based upon whether they degrade αor β linkages in agarose, breaking them into oligosaccharides. When secreted, α-agarases yield oligosaccharides with 3.6 anhydro-L-galactose at the reducing end whereas β-agarases result in D-galactose residues.http://www.creative-enzymes.com/product/Native-Pseudomonas-Atlantica-Agarase_1046.html

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Native Pseudomonas fragi Acyl-CoA Synthetase LAB GRADE 97%

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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Native Pseudomonas lemoignei ?-Hydroxybutyrate Dehydrogenase LAB GRADE 97%

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

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Native Pseudomonas sp. Acyl-coenzyme A Synthetase LAB GRADE 96%

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. Acyl coenzyme A synthetase proteins are involved in regulating and facilitating long-chain fatty acid transport in mammalian cells.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-Acylcoenzyme-A-Synthetase_1038.html

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Native Pseudomonas sp. Cholesterol Esterase LAB GRADE

Sterol esterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is steryl-ester acylhydrolase. This enzyme participates in bile acid biosynthesis.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-Cholesterol-Esterase_730.html
 

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Native Pseudomonas sp. Cholesterol Esterase LAB GRADE 97%

Sterol esterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is steryl-ester acylhydrolase. This enzyme participates in bile acid biosynthesis.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-Cholesterol-Esterase_730.html

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Native Pseudomonas sp. 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.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-Cholesterol-Oxidase_732.html
 

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Native Pseudomonas sp. Creatinine amidohydrolase LAB GRADE

Creatinine Amidohydrolase catalyzes the hydrolytic reaction converting creatinine to creatine. The enzyme is purified from a microorganism. The molecular size of the enzyme is approximately 175,000. The enzyme is useful for the enzy-matic assay of creatinine when coupled with other related enzymes. Creatinine + H2O → Creatine.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-Creatinine-Amidohydrolase_726.html
 

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