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| Product | Description | |
|---|---|---|
| carbamoyl-serine ammonia-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing CO2, ammonia, and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and a second ammonia molecule. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Group: Enzymes. Synonyms: O-carbamoyl-L-serine deaminase; carbamoylserine deaminase; O-carbamoyl-L-serine ammonia-lyase (pyruvate-forming). Enzyme Commission Number: EC 4.3.1.13. CAS No. 52227-64-2. 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-5273; carbamoyl-serine ammonia-lyase; EC 4.3.1.13; 52227-64-2; O-carbamoyl-L-serine deaminase; carbamoylserine deaminase; O-carbamoyl-L-serine ammonia-lyase (pyruvate-forming). Cat No: EXWM-5273. |  |
| D-serine ammonia-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC 4.2.1.14, D-serine dehydratase) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also acts, slowly, on D-threonine. Group: Enzymes. Synonyms: D-hydroxyaminoacid dehydratase; D-serine dehydrase; D-hydroxy amino acid dehydratase; D-serine hydrolase; D-serine dehydratase (deaminating); D-serine deaminase; D-serine hydro-lyase (deaminating). Enzyme Commission Number: EC 4.3.1.18. CAS No. 9015-88-7. 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-5278; D-serine ammonia-lyase; EC 4.3.1.18; 9015-88-7; D-hydroxyaminoacid dehydratase; D-serine dehydrase; D-hydroxy amino acid dehydratase; D-serine hydrolase; D-serine dehydratase (deaminating); D-serine deaminase; D-serine hydro-lyase (deaminating). Cat No: EXWM-5278. | |
| L-serine ammonia-lyase | Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead. The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13, L-serine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. This reaction is also carried out by EC 4.3.1.19, threonine ammonia-lyase, from a number of sources. Group: Enzymes. Synonyms: serine deaminase; L-hydroxyaminoacid dehydratase; L-serine deaminase; L-serine dehydratase; L-serine hydro-lyase (deaminating). Enzyme Commission Number: EC 4.3.1.17. CAS No. 9014-27-1. 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-5277; L-serine ammonia-lyase; EC 4.3.1.17; 9014-27-1; serine deaminase; L-hydroxyaminoacid dehydratase; L-serine deaminase; L-serine dehydratase; L-serine hydro-lyase (deaminating). Cat No: EXWM-5277. | |
| serine-sulfate ammonia-lyase | This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. Group: Enzymes. Synonyms: (L-SOS)lyase. Enzyme Commission Number: EC 4.3.1.10. CAS No. 9054-70-0. 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-5271; serine-sulfate ammonia-lyase; EC 4.3.1.10; 9054-70-0; (L-SOS)lyase. Cat No: EXWM-5271. | |
| 2-iminobutanoate/2-iminopropanoate deaminase | This enzyme, which has been found in all species and tissues examined, catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates. Group: Enzymes. Synonyms: yjgF (gene name); ridA (gene name); enamine/imine deaminase (ambiguous). Enzyme Commission Number: EC 3.5.99.10. 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-4586; 2-iminobutanoate/2-iminopropanoate deaminase; EC 3.5.99.10; yjgF (gene name); ridA (gene name); enamine/imine deaminase (ambiguous). Cat No: EXWM-4586. | |
| diaminopropionate ammonia-lyase | A pyridoxal phosphate enzyme. Active towards both D- and L-diaminopropanoate. D- and L-serine are poor substrates. Group: Enzymes. Synonyms: diaminopropionatase; α,β-diaminopropionate ammonia-lyase; 2,3-diaminopropionate ammonia-lyase; 2,3-diaminopropanoate ammonia-lyase; 2,3-diaminopropanoate ammonia-lyase (adding H2O; pyruvate-forming). Enzyme Commission Number: EC 4.3.1.15. CAS No. 51901-19-0. 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-5275; diaminopropionate ammonia-lyase; EC 4.3.1.15; 51901-19-0; diaminopropionatase; α,β-diaminopropionate ammonia-lyase; 2,3-diaminopropionate ammonia-lyase; 2,3-diaminopropanoate ammonia-lyase; 2,3-diaminopropanoate ammonia-lyase (adding H2O; pyruvate-forming). Cat No: EXWM-5275. | |
| histidine ammonia-lyase | This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.23 (tyrosine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. This enzyme catalyses the first step in the degradation of histidine and the product, urocanic acid, is further metabolized to glutamate. Group: Enzymes. Synonyms: histidase; histidinase; histidine α-deaminase; L-histidine ammonia-lyase. Enzyme Commission Number: EC 4.3.1.3. CAS No. 9013-75-6. 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-5289; histidine ammonia-lyase; EC 4.3.1.3; 9013-75-6; histidase; histidinase; histidine α-deaminase; L-histidine ammonia-lyase. Cat No: EXWM-5289. | |
| phenylalanine ammonia-lyase | This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase) and EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. The enzyme from some species is highly specific for phenylalanine. Group: Enzymes. Synonyms: phenylalanine deaminase; phenylalanine ammonium-lyase; PAL; L-phenylalanine ammonia-lyase; Phe ammonia-lyase. Enzyme Commission Number: EC 4.3.1.24. CAS No. 9024-28-6. PAL. 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-5284; phenylalanine ammonia-lyase; EC 4.3.1.24; 9024-28-6; phenylalanine deaminase; phenylalanine ammonium-lyase; PAL; L-phenylalanine ammonia-lyase; Phe ammonia-lyase. Cat No: EXWM-5284. | |
| phenylalanine/tyrosine ammonia-lyase | This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase), EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.24 (phenylalanine ammonia-lyase). The enzyme from some monocots, including maize, and from the yeast Rhodosporidium toruloides, deaminate L-phenylalanine and L-tyrosine with similar catalytic efficiency. The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. Group: Enzymes. Synonyms: PTAL; bifunctional PAL. Enzyme Commission Number: EC 4.3.1.25. 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-5285; phenylalanine/tyrosine ammonia-lyase; EC 4.3.1.25; PTAL; bifunctional PAL. Cat No: EXWM-5285. | |
| threo-3-hydroxy-D-aspartate ammonia-lyase | A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Delftia sp. HT23, also has activity against L-threo-3-hydroxyaspartate, L-erythro-3-hydroxyaspartate, and D-serine. Different from EC 4.3.1.20, erythro-3-hydroxy-L-aspartate ammonia-lyase and EC 4.3.1.16, threo-3-hydroxy-L-aspartate ammonia-lyase. Requires a divalent cation such as Mn2+, Co2+ or Ni2+. Group: Enzymes. Synonyms: D-threo-3-hydroxyaspartate dehydratase. Enzyme Commission Number: EC 4.3.1.27. 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-5286; threo-3-hydroxy-D-aspartate ammonia-lyase; EC 4.3.1.27; D-threo-3-hydroxyaspartate dehydratase. Cat No: EXWM-5286. | |
| threonine ammonia-lyase | Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead. The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16, threonine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase. Group: Enzymes. Synonyms: threonine deaminase; L-serine dehydratase; serine deaminase; L-threonine dehydratase; threonine dehydrase; L-threonine deaminase; threonine dehydratase; L-threonine hydro-lyase (deaminating); L-threonine . Enzyme Commission Number: EC 4.3.1.19. CAS No. 774231-81-1. 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-5279; threonine ammonia-lyase; EC 4.3.1.19; 774231-81-1; threonine deaminase; L-serine dehydratase; serine deaminase; L-threonine dehydratase; threonine dehydrase; L-threonine deaminase; threonine dehydratase; L-threonine hydro-lyase (deaminating); L-threonine ammonia-lyase. Cat No: EXWM-5279. | |
| Threonine Deaminase (Crude Enzyme) | Threonine ammonia-lyase, also commonly referred to as threonine deaminase or threonine dehydratase, is an enzyme responsible for catalyzing the conversion of L-threonine into alpha-ketobutyrate and ammonia. Alpha-ketobutyrate can be converted into L-isoleucine, so threonine ammonia-lyase functions as a key enzyme in BCAA synthesis. It employs a pyridoxal-5-phosphate cofactor, similar to many enzymes involved in amino acid metabolism. It is found in bacteria, yeast, and plants, though most research to date has focused on forms of the enzyme in bacteria. This enzyme was one of the first in which negative feedback inhibition by the end product of a metabolic pathway was directl...es. Synonyms: threonine deaminase; L-serine dehydratase; serine deaminase; L-threonine dehydratase; threonine dehydrase; L-threonine deaminase; threonine dehydratase; L-threonine hydro-lyase (deaminating); L-threonine ammonia-lyase. Enzyme Commission Number: EC 4.3.1.19. CAS No. 9024-34-4. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. threonine deaminase; L-serine dehydratase; serine deaminase; L-threonine dehydratase; threonine dehydrase; L-threonine deaminase; threonine dehydratase; L-threonine hydro-lyase (deaminating); L-threonine ammonia-lyase. Pack: 100ml. Cat No: NATE-1853. | |
| tryptophanase | A pyridoxal-phosphate protein, requiring K+. The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses 2,3-elimination and β-replacement reactions of some indole-substituted tryptophan analogues of L-cysteine, L-serine and other 3-substituted amino acids. Group: Enzymes. Synonyms: L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase. Enzyme Commission Number: EC 4.1.99.1. CAS No. 9024-00-4. TNase. 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-4925; tryptophanase; EC 4.1.99.1; 9024-00-4; L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase. Cat No: EXWM-4925. | |
| tyrosine ammonia-lyase | This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. The enzyme is far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides. Group: Enzymes. Synonyms: TAL; tyrase; L-tyrosine ammonia-lyase. Enzyme Commission Number: EC 4.3.1.23. CAS No. 1030840-68-6. 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-5283; tyrosine ammonia-lyase; EC 4.3.1.23; 1030840-68-6; TAL; tyrase; L-tyrosine ammonia-lyase. Cat No: EXWM-5283. | |
| tyrosine phenol-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-carbon bond, releasing phenol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme also slowly catalyses similar reactions with D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine. Group: Enzymes. Synonyms: β-tyrosinase; L-tyrosine phenol-lyase (deaminating). Enzyme Commission Number: EC 4.1.99.2. CAS No. 9059-31-8. 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-4933; tyrosine phenol-lyase; EC 4.1.99.2; 9059-31-8; β-tyrosinase; L-tyrosine phenol-lyase (deaminating). Cat No: EXWM-4933. | |
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