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| Product | Description | |
|---|---|---|
| alanine dehydrogenase | This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle (CO2 fixation). Group: Enzymes. Synonyms: AlaDH; L-alanine dehydrogenase; NAD-linked alanine dehydrogenase; α-alanine dehydrogenase; NAD-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1442; alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; L-alanine dehydrogenase; NAD-linked alanine dehydrogenase; α-alanine dehydrogenase; NAD-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: EXWM-1442. |  |
| Alanine Dehydrogenase (Crude Enzyme) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH 2 group of donors with NAD + or NADP + as acceptor. This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle (CO 2 fixation). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; synthesis; biotechnology; nutrition. Group: Enzymes. Synonyms: AlaDH; L-alanine dehydrogenase; NAD-linked alanine dehydrogenase; α-alanine dehydrogenase; NAD-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. AlaDH; L-alanine dehydrogenase; NAD-linked alanine dehydrogenase; α-alanine dehydrogenase; NAD-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Pack: 100ml. Cat No: NATE-1801. | |
| Alanine dehydrogenase, expressed in E. coli | Alanine dehydrogenase, expressed in E. coli is a microbial enzyme that catalyzes a reversible conversion of L-alanine to pyruvate [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9029-6-5. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P2854. |  |
| Alanine Dehydrogenase from Bacillus cereus, Recombinant | 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. Group: Enzymes. Synonyms: L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alan. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: > 350 units/ml. Storage: -20°C. Source: E. coli. Species: Bacillus cereus. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-0044. | |
| Alanine Dehydrogenase, recombinant | recombinant, expressed in E. coli, ?15 U/mg. Group: Fluorescence/luminescence spectroscopy. |  |
| Native Bacillus stearothermophilus Alanine Dehydrogenase | L-Alanine dehydrogenase is 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. Applications: The enzyme is useful for determination of l-alanine. Group: Enzymes. Synonyms: L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Mole weight: ca. 230,000; Subunit molecular weight : ca. 38,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-1899. | |
| Native Bacillus subtilis L-Alanine Dehydrogenase | 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-...genase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: Type I, ~30 units/mg protein (Lowry); Type II, > 20 units/mg protein (Lowry). Storage: -20°C. Form: Type I, buffered aqueous glycerol solution, Solution in 50% glycerol containing 10 mM potassium phosphate buffer, pH 7.7; Type II, ammonium sulfate suspension, Suspension in 2.4 M (NH4)2SO4 solution, pH 7.0. Source: Bacillus subtilis. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-0043. | |
| Native Sporosarcina sp. L-Phenylalanine Dehydrogenase | Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine EUR-dehydrogenase, and meso-a,EUR-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure. Applications: L-phenylalanine dehydrogenase is a nad+-dependent oxidoreductase that catalyzes the reversible, oxidative deamination of l-phenylalanine which results in its degradation. l-phenylalanine dehydrogenase is used to study phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis. Group: Enzymes. Synonyms: phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Enzyme Commission Number: EC 1.4.1.20. CAS No. 69403-12-9. PHD. Activity: > 6 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Sporosarcina sp. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-0558. | |
| Native Thermoactinomyces intermedius Phenylalanine Dehydrogenase | Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine EUR-dehydrogenase, and meso-a,EUR-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure. Group: Enzymes. Synonyms: phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Enzyme Commission Number: EC 1.4.1.20. CAS No. 69403-12-9. PHD. Mole weight: ca. 380,000; Subunit molecular weight : ca. 40,000. Appearance: Ammonium sulphate suspension. Storage: Stable at 0 to 4 °C for at least six months (Do not freeze). Source: Thermoactinomyces intermedius. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-1906. | |
| N-methylalanine dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-methyl-L-alanine:NADP+ oxidoreductase (demethylating, deaminating). Group: Enzymes. Enzyme Commission Number: EC 1.4.1.17. CAS No. 56379-51-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1450; N-methylalanine dehydrogenase; EC 1.4.1.17; 56379-51-2. Cat No: EXWM-1450. | |
| 3-hydroxypropionate dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxypropanoate:NAD+ oxidoreductase. This enzyme participates in beta-alanine metabolism and propanoate metabolism. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.59. CAS No. 9028-59-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0344; 3-hydroxypropionate dehydrogenase; EC 1.1.1.59; 9028-59-5. Cat No: EXWM-0344. | |
| alanopine dehydrogenase | In the reverse reaction, L-alanine can be replaced by L-cysteine, L-serine or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22 strombine dehydrogenase). Group: Enzymes. Synonyms: ALPDH alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase; meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase; alanopine: NAD oxidoreductase; ADH; alanopine:NAD oxidoreductase. Enzyme Commission Number: EC 1.5.1.17. CAS No. 71343-07-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1498; alanopine dehydrogenase; EC 1.5.1.17; 71343-07-2; ALPDH alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase; meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase; alanopine: NAD oxidoreductase; ADH; alanopine:NAD oxidoreductase. Cat No: EXWM-1498. | |
| D-Alanine 7-amido-4-methylcoumarin trifluoroacetate | D-Alanine 7-amido-4-methylcoumarin trifluoroacetate is a biochemical compound used in the biomedical industry serving as a substrate for enzyme assays, specifically for the detection of various enzymes involved in drug metabolism, such as dehydrogenases and decarboxylases. Synonyms: H-D-Ala-AMC TFA. CAS No. 201847-52-1. Molecular formula: C15H15F3N2O5. Mole weight: 360.29. |  |
| D-amino acid dehydrogenase (quinone) | An iron-sulfur flavoprotein (FAD). The enzyme from the bacterium Helicobacter pylori is highly specific for D-proline, while the enzyme from the bacterium Escherichia coli B is most active with D-alanine, D-phenylalanine and D-methionine. This enzyme may be the same as EC 1.4.99.6. Group: Enzymes. Synonyms: DadA. Enzyme Commission Number: EC 1.4.5.1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1486; D-amino acid dehydrogenase (quinone); EC 1.4.5.1; DadA. Cat No: EXWM-1486. | |
| dihydroanticapsin dehydrogenase | The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Group: Enzymes. Synonyms: BacC; ywfD (gene name). Enzyme Commission Number: EC 1.1.1.385. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0304; dihydroanticapsin dehydrogenase; EC 1.1.1.385; BacC; ywfD (gene name). Cat No: EXWM-0304. | |
| malonate-semialdehyde dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxopropanoate:NAD(P)+ oxidoreductase. This enzyme participates in beta-alanine metabolism. Group: Enzymes. Enzyme Commission Number: EC 1.2.1.15. CAS No. 9028-94-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1120; malonate-semialdehyde dehydrogenase; EC 1.2.1.15; 9028-94-8. Cat No: EXWM-1120. | |
| malonate-semialdehyde dehydrogenase (acetylating) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxopropanoate:NAD(P)+ oxidoreductase (decarboxylating, CoA-acetylating). This enzyme is also called malonic semialdehyde oxidative decarboxylase. This enzyme participates in 4 metabolic pathways: inositol metabolism, alanine and aspartate metabolism, beta-alanine metabolism, and propanoate metabolism. Group: Enzymes. Synonyms: malonic semialdehyde oxidative decarboxylase. Enzyme Commission Number: EC 1.2.1.18. CAS No. 9028-97-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1123; malonate-semialdehyde dehydrogenase (acetylating); EC 1.2.1.18; 9028-97-1; malonic semialdehyde oxidative decarboxylase. Cat No: EXWM-1123. | |
| opine dehydrogenase | In the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate. Group: Enzymes. Synonyms: (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming). Enzyme Commission Number: EC 1.5.1.28. CAS No. 108281-02-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1510; opine dehydrogenase; EC 1.5.1.28; 108281-02-3; (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming). Cat No: EXWM-1510. | |
| strombine dehydrogenase | Also catalyses the reaction of EC 1.5.1.17 alanopine dehydrogenase, but more slowly. Does not act on L-strombine. Group: Enzymes. Synonyms: strombine[N-(carboxymethyl)-D-alanine]dehydrogenase; N-(carboxymethyl)-D-alanine: NAD+ oxidoreductase. Enzyme Commission Number: EC 1.5.1.22. CAS No. 79393-84-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1504; strombine dehydrogenase; EC 1.5.1.22; 79393-84-3; strombine[N-(carboxymethyl)-D-alanine]dehydrogenase; N-(carboxymethyl)-D-alanine: NAD+ oxidoreductase. Cat No: EXWM-1504. | |
| tauropine dehydrogenase | In the reverse reaction, alanine can act instead of taurine, but more slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead of pyruvate. Group: Enzymes. Synonyms: 2-N-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming). Enzyme Commission Number: EC 1.5.1.23. CAS No. 104645-74-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1505; tauropine dehydrogenase; EC 1.5.1.23; 104645-74-1; 2-N-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming). Cat No: EXWM-1505. | |
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