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| Product | Description | |
|---|---|---|
| leucine dehydrogenase | Also acts on isoleucine, valine, norvaline and norleucine. Group: Enzymes. Synonyms: L-leucine dehydrogenase; L-leucine:NAD+ oxidoreductase, deaminating; LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. 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-1463; leucine dehydrogenase; EC 1.4.1.9; 9082-71-7; L-leucine dehydrogenase; L-leucine:NAD+ oxidoreductase, deaminating; LeuDH. Cat No: EXWM-1463. |  |
| Leucine dehydrogenase from Microorganism | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ ? 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Group: Enzymes. Synonyms: EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Mole weight: 43 kDa (SDS-PAGE). Activity: >500U/mg protein. Storage: Store at -20°C. Form: White powder, lyophilized. Source: Microorganism. EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH; LEDH. Cat No: NATE-1715. | |
| Leucine dehydrogenase, Microorganism | Leucine dehydrogenase, Microorganism (EC 1.4.1.9) can be purified from Bacillus spheroides. Leucine dehydrogenase catalyzed the oxidative deamination of L-leucine, L-valine, L-isoleucine, L-norvaline, L-alpha-aminobutyrate, and L-norleucine, and the reductive amination of their keto analogues [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: LDH, EC 1.4.1.9. CAS No. 9082-71-7. Pack Sizes: 1 KU; 100 U; 200 U. Product ID: HY-P2768. |  |
| L-leucine 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 product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Analysis; synthesis; biotechnology. Group: Enzymes. Synonyms: L-leucine dehydrogenase; L-leucine:NAD + oxidoreductase, deaminating; LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. L-leucine dehydrogenase; L-leucine:NAD + oxidoreductase, deaminating; LeuDH. Pack: 100ml. Cat No: NATE-1805. | |
| Native Bacillus cereus L-Leucine Dehydrogenase | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction:L-leucine + H2O + NAD+<-> 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Group: Enzymes. Synonyms: leucine dehydrogenase; L-leucine dehydrogenase; L-leucine:NAD+ oxidoreductase (deaminating); LeuDH; EC 1.4.1.9; 9082-71-7. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. Activity: 60-120 units/mg protein (Lowry). Storage: -20°C. Form: lyophilized powder. Source: Bacillus cereus. leucine dehydrogenase; L-leucine dehydrogenase; L-leucine:NAD+ oxidoreductase (deaminating); LeuDH; EC 1.4.1.9; 9082-71-7. Cat No: NATE-0391. | |
| Native Bacillus sp. Leucine dehydrogenase | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ <-> 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Applications: This enzyme is useful for enzyme determination of l-leucine and the activity of leucine amino-peptidase. Group: Enzymes. Synonyms: EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. Mole weight: 245 kDa. Activity: Grade? 20U/mg-solid or more (containing approx. 70% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Source: Bacillus sp. EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Cat No: DIA-209. | |
| Native Bacillus stearothermophilus Leucine Dehydrogenase | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ <-> 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Applications: The enzyme is useful for determination of l-leucine, l-valine or l-isoleucine. Group: Enzymes. Synonyms: EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. Mole weight: ca. 300,000; Subunit molecular weight : ca. 49,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Cat No: NATE-1905. | |
| 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) | Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168. Group: Enzymes. Synonyms: 2-oxoisocaproate dehydrogenase; 2-oxoisovalerate (lipoate) dehydrogenase; 3-methyl-2-oxobutanoate dehydrogenase (lipoamide); 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and acceptor-2-methylpropanoylating); α-keto-α-methylvalerate dehydrogenase; α. Enzyme Commission Number: EC 1.2.4.4. CAS No. 9082-72-8. 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-1219; 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring); EC 1.2.4.4; 9082-72-8; 2-oxoisocaproate dehydrogenase; 2-oxoisovalerate (lipo | |
| aspartate-semialdehyde dehydrogenase | In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it. Group: Enzymes. Synonyms: aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Enzyme Commission Number: EC 1.2.1.11. CAS No. 9000-98-0. 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-1117; aspartate-semialdehyde dehydrogenase; EC 1.2.1.11; 9000-98-0; aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Cat No: EXWM-1117. | |
| dihydrolipoyllysine-residue (2-methylpropanoyl)transferase | A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine. Group: Enzymes. Synonyms: dihydrolipoyl transacylase; enzyme-dihydrolipo. Enzyme Commission Number: EC 2.3.1.168. CAS No. 102784-26-9. 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-2108; dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; EC 2.3.1.168; 102784-26-9; dihydrolipoyl transacylase; enzyme-dihydrolipoyllysine:2-methylpropanoyl-CoA S-(2-methylpropanoyl)transferase; 2-methylpropanoyl-CoA:enzyme-6-N-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase. Cat No: EXWM-2108. | |
| Glutamate Dehydrogenase (NAD(P)) from E.coli, Recombinant | 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. Applications: Use recombinant glutamate dehydrogenase in diagnostic tests for the determination of ammonia, urea, l-glutamate, glutamate pyruvate transaminase and leucine aminopeptidase. Group: Enzymes. Synonyms: glu. CAS No. 9029-12-3. GLDH. Mole weight: ~2 200 kD for the associated enzyme with 8 subunits; 280 kD for one subunit. Activity: >80 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: E.coli. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-0981. | |
| Glutamate dehydrogenase, Recombinant | 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. Glutamate dehydrogenase (gldh, ec 1.4.1.2) is the enzyme present in the mitochondrial matrix of the cell. it can convert glutamic acid to α-ketoglutarate and catalyze the re...ations: Except glutamate dehydrogenation, gldh can also catalytic the deaminase of other amino acids such as l-valine, l-2-aminobutyric acid and l-leucine. the main measuring method is continuous monitoring. moreover, gldh catalyzes the reaction of α-ketoglutarate, h+,ammonia and nadh to generating glutamic. since nadh is the color source of many biochemical assays, therefore the reaction catalyzed by the corresponding gldh is widely used to detect the final step of biochemical detection reagent. Group: Enzymes. Synonyms: glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate | |
| Isovaleryl-L-carnitine chloride | Isovaleryl-L-carnitine is a naturally occurring acylcarnitine metabolized from leucine via a deficiency of the mitochondrial enzyme isovaleryl-CoA dehydrogenase, which results in an accumulation of derivatives of isovaleryl-CoA. Synonyms: L-Isovalerylcarnitine; [(2R)-3-carboxy-2-(3-methylbutanoyloxy)propyl]-trimethylazanium chloride. Grades: ≥95%. CAS No. 139144-12-0. Molecular formula: C12H24NO4·Cl. Mole weight: 281.78. |  |
| Native Candida boidinii Formate Dehydrogenase | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Fdh is an abundant enzyme from yeast candida boidinii (cbfdh) that plays an important role in the energy supply of methylotrophic microorganisms and in the stress response of plants. Applications: Formate dehydrogenase (fdh) is used for diagnostics in large scale industrial pr ocesses. its used in the production of an unnatural amino acid, tert-l-leucine, a component of some hiv protease and matrix metalloprotease inhibitors. Group: Enzymes. Synonyms: EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. FDH. Activity: Type I, 5.0-15.0 units/mg protein; Type II, 0.3-0.6 units/mg; Type III, ~50 U/mL. Storage: -20°C. Form: Type I, lyophilized powder; Type II, powder; Type III, clear brown liquid. Source: Candida boidinii. EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: NATE-0254. | |
| Native Microorganism Glutamate Dehydrogenase (NAD-dependent) | 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. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urea...ating); EC 1.4.1.2; GLDH. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. Mole weight: approx. 260 kDa. Activity: 100 U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Glutamate Dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; NAD: gluta | |
| Native Proteus sp. Glutamate Dehydrogenase (NADP-dependent) | 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. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urea...lutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Enzyme Commission Number: EC 1.4.1.4. Mole weight: approx. 300 kDa. Activity: 300U/mg-protein or more (9,000U/ml or more). Appearance: Solution with 50mM Tris-HCl buffer containing 0.05% NaN3 and 5.0mM EDTA, pH 7.8. Form: Freeze dried powder. Source: Proteus sp. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: DIA-196. | |
| Native Proteus sp. L-Glutamic Dehydrogenase (NADP) | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urease. this enzyme is also used for enzymatic determination of urea when coupled with urease (urh-201) in clinical analysis. Group: Enzymes. Synonyms: L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate de. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Mole weight: mol wt ~300 kDa. Activity: > 400 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous solution; Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide. Source: Proteus sp. L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: NATE-0395. | |
| 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. | |
| 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. | |
| QL9 | QL9 (QLSPFPFDL), derived from the enzyme 2-oxoglutarate dehydrogenase, is a high-affinity alloantigen for the 2C T cell receptor (TCR). Synonyms: L-Leucine, L-glutaminyl-L-leucyl-L-seryl-L-prolyl-L-phenylalanyl-L-prolyl-L-phenylalanyl-L-α-aspartyl-; Gln-Leu-Ser-Pro-Phe-Pro-Phe-Asp-Leu; QL 9; QL-9. Grades: ≥95%. CAS No. 159646-83-0. Molecular formula: C52H74N10O14. Mole weight: 1063.21. | |
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