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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 sphaericus 12?-Hydroxysteroid Dehydrogenase LAB GRADE 97%

In enzymology, a 12alpha-hydroxysteroid dehydrogenase (EC 1.1.1.176) is an enzyme that catalyzes the chemical reaction:3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NADP+↔ 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+. Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and NADP+, whereas its 3 products are 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme is involved in a metabolic pathway that degrades bile acids into cholesterol.http://www.creative-enzymes.com/product/Native-Bacillus-Sphaericus-12-Hydroxysteroid-Dehydrogenase_1661.html

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Native Bacillus stearothermophilus Acetate Kinase LAB GRADE 97%

In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation. Short-chain fatty acids (SCFAs) play a major role in carbon cycle and can be utilized as a source of carbon and energy by bacteria. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydRate. A related enzyme, butyRate kinase, facilitates the formation of butyryl-CoA by phosphorylating butyRate in the presence of ATP to form butyryl phosphatehttp://www.creative-enzymes.com/product/Native-Bacillus-Stearothermophilus-Acetate-Kinase_1034.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 Bacillus stearothermophilus Myokinase LAB GRADE 97%

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

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Native Bacillus stearothermophilus Phosphoglucose isomerase LAB GRADE

Glucose-6-phosphate isomerase is an enzyme that catalyzes the conversion of glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis. The human variant of this enzyme is encoded by the GPI gene.http://www.creative-enzymes.com/product/Native-Bacillus-Stearothermophilus-Phosphoglucose-Isomerase_758.html
 

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Native Bacillus stearothermophilus Phosphoglucose isomerase LAB GRADE 97%

Glucose-6-phosphate isomerase is an enzyme that catalyzes the conversion of glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis. The human variant of this enzyme is encoded by the GPI gene.http://www.creative-enzymes.com/product/Native-Bacillus-Stearothermophilus-Phosphoglucose-Isomerase_758.html

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Native Bacillus subtilis Bilirubin oxidase LAB GRADE

In enzymology, a bilirubin oxidase (EC 1.3.3.5) is an enzyme that catalyzes the chemical reaction 2 bilirubin + O2↔ 2 biliverdin + 2 H2O. Thus, the two substrates of this enzyme are bilirubin and O2, whereas its two products are biliverdin and H2O. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in porphyrin and chlorophyll metabolism.http://www.creative-enzymes.com/product/Native-Bacillus-Subtilis-Bilirubin-Oxidase_725.html
 

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Native Bacillus subtilis L-Alanine Dehydrogenase LAB GRADE 97%

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/Native-Bacillus-Subtilis-LAlanine-Dehydrogenase_1246.html

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Native Bacteria Achromopeptidase LAB GRADE 96%

Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus.http://www.creative-enzymes.com/product/Native-Bacteria-Achromopeptidase_948.html

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