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

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 Microorganism N-Acetylneuraminic acid aldolase LAB GRADE

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 Microorganism P-hydroxybenzoate hydroxylase LAB GRADE 97%

In enzymology, a 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) is an enzyme that catalyzes the chemical reaction: 4-hydroxybenzoate + NADPH + H+ + O2 ↔ protocatechuate + NADP+ + H2O. The 4 substrates of this enzyme are 4-hydroxybenzoate, NADPH, H+, and O2, whereas its 3 products are protocatechuate, NADP+, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.http://www.creative-enzymes.com/product/Native-Microorganism-Phydroxybenzoate-Hydroxylase_799.html

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Native Sweet Potato Non-Prostatic Acid Phosphatase LAB GRADE 97%

Acid phosphatase is a phosphatase, a type of enzyme, used to free attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase. Acid phosphatase is stored in lysosomes and functions when these fuse with endosomes, which are acidified while they function; therefore, it has an acid pH optimum. This enzyme is present in many animal and plant species. Different forms of acid phosphatase are found in different organs, and their serum levels are used to evaluate the success of the surgical treatment of prostate cancer. In the past, they were also used to diagnose this type of cancer.http://www.creative-enzymes.com/product/Native-Sweet-Potato-NonProstatic-Acid-Phosphatase_1514.html

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Native Bacillus sp. Purine Nucleoside Phosphorylase LAB GRADE 97%

Purine nucleoside phosphorylase (also known as PNPase) is an enzyme (EC 2.4.2.1) involved in purine metabolism. PNP metabolizes adenosine into adenine, inosine into hypoxanthine, and guanosine into guanine, in each case creating ribose phosphate. NP encodes the enzyme purine nucleoside phosphorylase that together with adenosine deaminase (ADA) serves a key role in purine catabolism, referred to as the salvage pathway. Mutations in either enzyme result in a severe combined immunodeficiency (SCID). Confusingly, the same abbreviation (PNPase), is also used for another, otherwise unrelated, enzyme, namely Polynucleotide Phosphorylase.http://www.creative-enzymes.com/product/Native-Bacillus-Sp-Purine-Nucleoside-Phosphorylase_760.html

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Native Bacillus stearothermophilus Alanine Racemase LAB GRADE 97%

Alanine racemase is involved in alanine, aspartate and D-alanine metabolism. 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit alanine racemase. Alanine racemase monomer is composed of two domains, an eight-stranded α/β barrel at the N-terminus and a C-terminal domain. The N-terminus includes residues 1-240, whereas the C-terminal comprises of the β-strand (residues 241-388). One molecule of pyridoxalphosphate (PLP) is present as the cofactor in each subunit.http://www.creative-enzymes.com/product/Native-Bacillus-Stearothermophilus-Alanine-Racemase_1047.html

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Native Microorganism Glucose-6-phosphate Dehydrogenase LAB GRADE

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-Microorganism-Glucose6phosphate-Dehydrogenase_741.html
 

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Native Pediococcus sp. Glycerol-3-phosphate oxidase LAB GRADE 97%

In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction: sn-glycerol 3-phosphate + O2↔ glycerone phosphate + H2O2. Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2.http://www.creative-enzymes.com/product/Native-Pediococcus-Sp-Glycerol3phosphate-Oxidase_750.html

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Native Pediococcus sp. L-?-glycerophosphate oxidase LAB GRADE 97%

In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction: sn-glycerol 3-phosphate + O2 ↔ glycerone phosphate + H2O2. Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD.http://www.creative-enzymes.com/product/Native-Pediococcus-Sp-L-glycerophosphate-Oxidase_795.html

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Alanine Dehydrogenase from Bacillus cereus, recombinant LAB GRADE

L-Alanine dehydrogenase is an A-stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the geneRation of pyruvate during sporulation. L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD binds before L-alanine. Subsequently, ammonia, pyruvate, and NADH are released in that specific order. Optimal pH for the amination reaction is 8.8-9.0, whereas it is 10-10.5 for the deamination reaction. The enzyme is inactivated by divalent metal ions and p-chloromercuribenzoate, mercuric ion being most effective. The inactivation may be reversed by L-or D-cysteine.http://www.creative-enzymes.com/product/Alanine-Dehydrogenase-From-Bacillus-Cereus-Recombinant_1712.html
 

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