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Native Microorganism Phosphoenolpyruvate carboxylase LAB GRADE 96%

Phosphoenolpyruvate carboxylase is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO3−) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate: PEP + HCO3-→ oxaloacetate + Pi. This reaction is used for carbon fixation in CAM (crassulacean acid metabolism) and C4 organisms, as well as to regulate flux through the citric acid cycle (also known as Krebs or TCA cycle) in bacteria and plants. The enzyme structure and its two step catalytic, irreversible mechanism have been well studied. PEP carboxylase is highly regulated, both by phosphorylation and allostery.http://www.creative-enzymes.com/product/Native-Microorganism-Phosphoenolpyruvate-Carboxylase_808.html

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Native Microorganism Purine-nucleoside phosphorylase LAB GRADE 97%

In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction: purine nucleoside + phosphate ↔ purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases.http://www.creative-enzymes.com/product/Native-Microorganism-Purinenucleoside-Phosphorylase_812.html

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Native Pseudomonas sp. Protocatechuate 3, 4-dioxygenase LAB GRADE

In enzymology, a protocatechuate 3,4-dioxygenase (EC 1.13.11.3) is an enzyme that catalyzes the chemical reaction: 3,4-dihydroxybenzoate + O2 ↔ 3-carboxy-cis,cis-muconate. Thus, the two substrates of this enzyme are 3,4-dihydroxybenzoate (protocatechuic acid) and O2, whereas its product is 3-carboxy-cis,cis-muconate. This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, iron.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-Protocatechuate-3-4dioxygenase_810.html
 

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Native Bacillus sp. Glucose-6-phosphate dehydrogenase LAB GRADE 97%

Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is an cytosolic enzyme that catalyzes the chemical reaction: D-glucose 6-phosphate + NADP+↔ 6-phospho-D-glucono-1, 5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway (see image), a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH).http://www.creative-enzymes.com/product/Native-Bacillus-Sp-Glucose6phosphate-Dehydrogenase_739.html

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Native Flavobacterium sp. Proline specific endopeptidase LAB GRADE

Prolyl endopeptidase (PE) also known as prolyl oligopeptidase or post-proline cleaving enzyme is an enzyme that in humans is encoded by the PREP gene.http://www.creative-enzymes.com/product/Native-Flavobacterium-Sp-Proline-Specific-Endopeptidase_809.html
 

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Native Gluconobacter industrius D-Fructose Dehydrogenase LAB GRADE

D-fructose dehydrogenase is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively.http://www.creative-enzymes.com/product/Native-Gluconobacter-Industrius-DFructose-Dehydrogenase_1714.html
 

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Native Microorganism N-Acetylneuraminic acid aldolase LAB GRADE 97%

In enzymology, a N-acetylneuraminate lyase (EC 4.1.3.3) is an enzyme that catalyzes the chemical reaction: N-acetylneuraminate ↔ N-acetyl-D-mannosamine + pyruvate. Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and pyruvate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds.http://www.creative-enzymes.com/product/Native-Microorganism-NAcetylneuraminic-Acid-Aldolase_778.html

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Native Pseudomonas sp. D-3-hydroxybutyrate dehydrogenase LAB GRADE

In enzymology, a 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) is an enzyme that catalyzes the chemical reaction: (R)-3-hydroxybutanoate + NAD+ ↔ acetoacetate + NADH + H+. Thus, the two substrates of this enzyme are (R)-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in synthesis and degradation of ketone bodies and butanoate metabolism.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-D3hydroxybutyrate-Dehydrogenase_800.html
 

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Native Saccharomyces cerevisiae Alcohol Dehydrogenase LAB GRADE 97%

Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.http://www.creative-enzymes.com/product/Native-Saccharomyces-Cerevisiae-Alcohol-Dehydrogenase_1048.html

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3-Acetylpyridine-Adenine Dinucleotide, Oxidized (APAD) LAB GRADE 97%

Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.http://www.creative-enzymes.com/product/3AcetylpyridineAdenine-Dinucleotide-Oxidized-APAD-_1507.html

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