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| Product | Description | |
|---|---|---|
| sarcosine oxidase | A flavoprotein (FAD). The flavin is both covalently and non-covalently bound in a molar ratio of 1:1. Group: Enzymes. Enzyme Commission Number: EC 1.5.3.1. CAS No. 9029-22-5. SAO. 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-1537; sarcosine oxidase; EC 1.5.3.1; 9029-22-5. Cat No: EXWM-1537. |  |
| Sarcosine oxidase, Bacillus | Sarcosine oxidase, Bacillus (SAO) can catalyze the oxidative demethylation of sarcosine to generate glycine, H 2 O 2 , 5,10-CH 2 -tetrahydrofolate, which are often used in biochemical reactions [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: SAO. CAS No. 9029-22-5. Pack Sizes: 10 KU. Product ID: HY-P2861. |  |
| Sarcosine Oxidase from E. coli, Recombinant | Sarcosine oxidase (SAO) is an enzyme that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5, 10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. sarcosine + H2O + O2=glycine + formaldehyde + H2O2. Group: Enzymes. Synonyms: Sarcosine Oxidase; EC 1.5.3.1; SAO. Enzyme Commission Number: EC 1.5.3.1. Mole weight: ca. 49 kDa. Activity: > 10 U/mg. Appearance: Yellow lyophilizate. Storage: at -20°C. Source: E. coli. Species: E. coli. Sarcosine Oxidase; EC 1.5.3.1; SAO. Cat No: DIA-414. | |
| Native Bacillus sp. Sarcosine Oxidase | Sarcosine oxidase is an enzyme (EC 1.5.3.1) that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5,10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. Corynebacterial sarcosine oxidase is a heterotetramer and is produced as an inducible enzyme when Corynebacterium sp.is grown with sarcosine as source of carbon and energy. Monomeric sarcosine oxidase (msox) is a flavoenzyme that catalyzes the oxidative demethylation of sarcosine (n-methylglycine) to yield glycine, formaldehyde, and hydrogen peroxide. monomeric sarcosine oxidase can oxidize other secondary amino acids such as n-methyl-l-alanine, n-ethylglycine, and l-proline. Applications: Sarcosine oxidase has been used in a study as part of a multienzyme cascade, that when immobilized constructed amperometric biosensors. sarcosine oxidase has also been used in a study to investigate oxidation of amines by flavoproteins. Group: Enzymes. Synonyms: Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Enzyme Commission Number: EC 1.5.3.1. CAS No. 9029-22-5. SAO. Activity: 25-50 units/mg solid. Storage: -20°C. Form: lyophilized powder; No stabilizers added. Source: Bacillus sp. Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Cat No: NATE-0664. | |
| Native E.coli Sarcosine Oxidase | Oxidoreductase that catalyzes the demethylation of sarcosine to glycine. Use Sarcosine Oxidase in your preferred creatinine reagent mix and rely on the proven diagnostic quality of this product. Applications: Use sarcosine oxidase in diagnostic tests for the determination of creatinine. this can be done using one of two methods: (1) in combination with creatinase and creatininase. (2) in combination with creatinine deaminase, n-carbamoylsarcosine amidase and n-methylhydantoinase (atp-hydrolyzing). Group: Enzymes. Synonyms: Sarcosine Oxidase; SAO. CAS No. 9029-22-5. SAO. Mole weight: 40 kD. Activity: 22-40 U/mg lyophilizate; >45 U/mg protein. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: Yellow lyophilizate. Source: E. coli. Sarcosine Oxidase; EC 1.5.3.1; SAO. Cat No: DIA-290. | |
| Native Microorganism Sarcosine Oxidase | Sarcosine oxidase (SAO) is an enzyme that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5, 10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. sarcosine + H2O + O2 = glycine + formaldehyde + H2O2. Applications: This enzyme is useful for enzymatic determination of creatinine, creatine, and sarcosine when coupling with creatinine amidohydrolase and creatine amidinohydrolase.-341 is newer type of sarosine oxidase, with improved stability in antimicrobial reagent. Group: Enzymes. Synonyms: Sarcosine Oxidase; EC 1.5.3.1; SAO. Enzyme Commission Number: EC 1.5.3.1. CAS No. 9029-22-5. SAO. Mole weight: approx. 65 kDa (by gel filtration). Activity: Grade? 8.0U/mg-solid or more. Stability: Stable at-20°C for at least one year. Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Sarcosine Oxidase; EC 1.5.3.1; SAO. Cat No: DIA-171. | |
| betaine-aldehyde dehydrogenase | In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase). In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). Group: Enzymes. Synonyms: betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB. Enzyme Commission Number: EC 1.2.1.8. CAS No. 9028-90-4. 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-1182; betaine-aldehyde dehydrogenase; EC 1.2.1.8; 9028-90-4; betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB. Cat No: EXWM-1182. | |
| betaine reductase | The reaction is observed only in the direction of betaine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for betaine binding and trimethylamine release. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.2 (glycine reductase) and EC 1.21.4.3 (sarcosine reductase). Group: Enzymes. Synonyms: acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (N,N,N-trimethylglycine-forming). Enzyme Commission Number: EC 1.21.4.4. CAS No. 125752-87-6. 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-1259; betaine reductase; EC 1.21.4.4; 125752-87-6; acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (N,N,N-trimethylglycine-forming). Cat No: EXWM-1259. | |
| choline monooxygenase | The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase). The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). Group: Enzymes. Enzyme Commission Number: EC 1.14.15.7. CAS No. 118390-76-4. 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-0950; choline monooxygenase; EC 1.14.15.7; 118390-76-4. Cat No: EXWM-0950. | |
| dimethylglycine oxidase | A flavoprotein (FAD). Does not oxidize sarcosine. Group: Enzymes. Enzyme Commission Number: EC 1.5.3.10. CAS No. 37256-30-7. 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-1538; dimethylglycine oxidase; EC 1.5.3.10; 37256-30-7. Cat No: EXWM-1538. | |
| Dimethylglycine oxidase from Arthrobacter globifomis, Recombinant | Dimethylglycine oxidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative demethylation of dimethylglycine to yield sarcosine, formaldehyde, and hydrogen peroxide. The N-terminal region binds FAD covalently so it is yellowish. Dimethylglycine oxidase recombinant originated from arthrobacter globifomis fused to his tag at n-terminal produced in e. coli is a single, non-glycosylated, polypeptide chain containing 850 amino acids and having a molecular mass of 92.1 kda. the dmgo is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: DMGO; Dimethylglycine Oxidase. CAS No. 74870-79-4. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. DMGO. Mole weight: 92.1 kDa. Stability: Dimethylglycine Oxidase Recombinant although stable at 4°C for 30 days, should be stored desiccated below -20°C for periods greater than 30 days. Please prevent freeze-thaw cycles. Appearance: Sterile filtered liquid formulation 1 mg/ml. Source: E. coli. Species: Arthrobacter globifomis. DMGO; Dimethylglycine Oxidase. Cat No: NATE-0826. | |
| glycine oxidase | A flavoenzyme containing non-covalently bound FAD. The enzyme from Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine, D-alanine, D-α-aminobutyrate, D-proline, D-pipecolate and N-methyl-D-alanine. It differs from EC 1.4.3.3, D-amino-acid oxidase, due to its activity on sarcosine and D-pipecolate. The intermediate 2-iminoacetate is used directly by EC 2.8.1.10, thiazole synthase. Group: Enzymes. Enzyme Commission Number: EC 1.4.3.19. CAS No. 39307-16-9. 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-1473; glycine oxidase; EC 1.4.3.19; 39307-16-9. Cat No: EXWM-1473. | |
| Glycine Oxidase H244K from Bacillus subtilis, recombinant | Glycine oxidase (GO) from Bacillus subtilis (EC 1.4.3.19) is a homotetrameric flavin-dependent oxidoreductase. Each GO monomer is non-covalently bound to flavin adenine dinucleotide. GO catalyzes oxidative deamination of various primary and secondary amines (e.g. glycine, sarcosine, N-ethylglycine) and some D-amino acids (e.g. D -alanine, D -proline, D -valine) to the corresponding α-keto acids and hydrogen peroxide. Primarily, glycine oxidase catalyzes the oxidation of glycine in the biosynthesis of thiamine. The variant H244K shows a higher substrate specificity ratio for glycine versus sarcosine and a 5-fold improved specific activity in comparison to the wild-type. Group: Enzymes. Synonyms: Glycine oxidase; glycine oxygen oxidoreductase (deaminating); GO; EC 1.4.3.19; 39307-16-9. Enzyme Commission Number: EC 1.4.3.19. CAS No. 39307-16-9. Purity: > 90% by SDS-PAGE. Mole weight: 43.1 kDa (1-369 aa, NT His Tag). Activity: 1200 mU/mg. Storage: Store at -20°C. Stable for at least 1 year as supplied. Avoid repeated freeze and thaw cycles. Form: Liquid. Source: E. coli. Species: Bacillus subtilis. Glycine oxidase; glycine oxygen oxidoreductase (deaminating); GO; EC 1.4.3.19; 39307-16-9. Cat No: NATE-1674. | |
| N-alkylglycine oxidase | Isolated from the mold Cladosporium sp. G-10. Acts on N6-(carboxymethyl)lysine, 6-[(carboxymethy)amino]hexanoic acid, sarcosine and N-ethylglycine. It has negligible action on glycine (cf. EC 1.4.3.19 glycine oxidase). Group: Enzymes. Synonyms: N-carboxymethylalkylamine:oxygen oxidoreductase (decarboxymethylating). Enzyme Commission Number: EC 1.5.3.20. 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-1548; N-alkylglycine oxidase; EC 1.5.3.20; N-carboxymethylalkylamine:oxygen oxidoreductase (decarboxymethylating). Cat No: EXWM-1548. | |
| Native Actinobacillus sp. Creatinase | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction:creatine + H2O? sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. Creatinase accelerates the conversion reaction of creatine and water molecule to sarcosine and urea. It always acts in homodimer state and is induced by choline chloride. Applications: Creatinase mixed with sarcosine oxidase may be used to determine the level of creatine in different ph, temperature, enzyme ratio, and buffer concentration. it may also be used to determine the plasma creatinine level by using a centrifugal analyser. Group: Enzymes. Synonyms: Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Mole weight: mol wt ~100 kDa. Activity: 6.0 U/mg-solid or more. Storage: -20°C. Form: Lyophilized powder containing sugars and EDTA as stabilizers. Source: Actinobacillus sp. Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Cat No: NATE-0160. | |
| Native Corynebacterium lilium Creatinine Deiminase | Hydrolase for creatinine determination that catalyzes the conversion of creatinine to N-methylhydantoin and ammonia. Rely on the proven diagnostic quality of this product. Applications: Use creatinine deaminase in diagnostic tests for the determination of creatinine in combination with n-carbamoylsarcosine amidase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: Creatinine hydrolase; creatinine desiminase. Creatinine Deiminase. Activity: 45.0-90.0 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Protect from light. Appearance: Beige lyophilizate. Source: Corynebacterium lilium. Creatinine hydrolase; Creatinine deaminase; EC 3.5.4.21; creatinine desiminase. Cat No: DIA-291. | |
| Native E. coli N-Carbamoylsarcosine Amidase | In enzymology, a N-carbamoylsarcosine amidase is an enzyme that catalyzes the chemical reaction: N-carbamoylsarcosine + H2O rightleftharpoons sarcosine + CO2 + NH3. Thus, the two substrates of this enzyme are N-carbamoylsarcosine and H2O, whereas its 3 products are sarcosine, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in arginine and proline metabolism. Hydrolase that catalyzes the interconversion of n-carbamoylsarcosine to sarcosine. Applications: Use n-carbamoylsarcosine amidase in diagnostic tests for the determination of creatinine in combination with creatinine deaminase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. CAS No. 92767-52-7. N-Carbamoylsarcosine Amidase. Activity: 0.80-1.30 U/mg. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: White lyophilizate. Source: E. coli. Species: E. coli. N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. Cat No: NATE-0876. | |
| Native Microorganism Creatine Amidinohydrolase | Creatine Amidinohydrolase catalyzes the hydrolytic reaction converting creatine to sarcosine and urea. The enzyme is purified from a microorganism. The molecular weight of the enzyme is approximately 67,000. The enzyme is useful for the enzymatic assay of creatine and creatinine when coupled with other related enzymes. creatine + H2O ? sarcosine + urea. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatinine amidohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: Creatine Amidinohydrolase; Creatinase; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Creatinase. Mole weight: approx. 67 kDa (by gel filtration). Activity: Grade? 4.0 U/mg-solid or more. Stability: Stable at -20°C for at least one year. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Cat No: DIA-185. | |
| Native Microorganism Creatine Amidohydrolase | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction: creatine + H2O ?sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. The native enzyme was shown to be made up of two subunit monomers via SDS-polyacrylamide gel electrophoresis. Creatinase has been found to be most active at pH 8 and is most stable between ph 6-8 for 24 hrs. at 37 degrees. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. This enzyme participates in arginine and proline metabolism. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Mole weight: approx. 67 kDa (by gel filtration). Activity: 4.0 U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Cat No: DIA-185. | |
| Native microorganisms Creatininase | Creatininase from Pseudomonas sp. is a homohexameric enzyme with a molecular mass of 28.4 kDa per subunit. It is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. Each monomer contains a binuclear zinc centre near the C termini of the β-strands and the N termini of the main α-helices. These zinc ions indicate the location of the active site. Protein determined by biuret. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Enzyme Commission Number: EC 3.5.2.10. CAS No. 9025-13-2. Creatininase. Mole weight: mol wt ~175 kDa. Activity: 100-300 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing sucrose and BSA as stabilizers. Source: microorganisms. EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Cat No: NATE-0163. | |
| Native Pseudomonas sp. Creatinine amidohydrolase | Creatinine Amidohydrolase catalyzes the hydrolytic reaction converting creatinine to creatine. The enzyme is purified from a microorganism. The molecular size of the enzyme is approximately 175,000. The enzyme is useful for the enzy-matic assay of creatinine when coupled with other related enzymes. Creatinine + H2O ? Creatine. Creatininase from pseudomonas sp. is a homohexameric enzyme with a molecular mass of 28.4 kda per subunit. it is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. each monomer contains a binuclear zinc centre near the c termini of the β-strands and the n termini of the main α-helices. these zinc ions indicate the location of the active site. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: creatininase; creatinine hydrolase; creatinine . Enzyme Commission Number: EC 3.5.2.10. CAS No. 9025-13-2. Creatininase. Mole weight: 175 kDa. Activity: > 250U/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing sucrose and BSA as stabilizers. Source: Pseudomonas sp. creatininase; creatinine hydrolase; creatinine amidohydrolase; EC 3.5.2.10; 9025-13-2. Cat No: DIA-130. | |
| Native Pseudomonas sp. Sarcosine Dehydrogenase | In enzymology, sarcosine dehydrogenase (EC 1.5.99.1) is a mitochondrial enzyme that catalyzes the chemical reaction N-demethylation of sarcosine to give glycine. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. Sarcosine dehydrogenase is closely related to dimethylglycine dehydrogenase, which catalyzes the demethylation reaction of dimethylglycine to sarcosine. Both sarcosine dehydrogenase and dimethylglycine dehydrogenase use FAD as a cofactor. Sarcosine dehydrogenase is linked by electron-transferring flavoprotein (ETF) to the respiratory redox chain. Group: Enzymes. Synonyms: sarcosine dehydrogenase; EC 1.5.99.1; sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine: (acceptor) oxidoreductase (demethylating); 37228-65-2; EC 1.5.8.3. Enzyme Commission Number: EC 1.5.99.1. CAS No. 37228-65-2. Sarcosine dehydrogenase. Activity: 0.5-1.5 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing approx. 60% sucrose, 10% potassium phosphate buffer salts and trace EDTA. Source: Pseudomonas sp. sarcosine dehydrogenase; EC 1.5.99.1; sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine: (acceptor) oxidoreductase (demethylating); 37228-65-2; EC 1.5.8.3. Cat No: NATE-0663. | |
| N-Methylhydantoinase (ATP-hydrolyzing) from Arthrobacter sp., Recombinant | In enzymology, a N-methylhydantoinase (ATP-hydrolysing) is an enzyme that catalyzes the chemical reaction: ATP + N-methylimidazolidine-2,4-dione + 2 H2O rightleftharpoons ADP + phosphate + N-carbamoylsarcosine. The 3 substrates of this enzyme are ATP, N-methylimidazolidine-2,4-dione, and H2O, whereas its 3 products are ADP, phosphate, and N-carbamoylsarcosine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. This enzyme participates in arginine, creatinine, and proline metabolism. Hydrolase for creatinine determination that uses atp to catalyze the conversion of...amoylsarcosine amidase and sarcosine oxidase. Group: Enzymes. Synonyms: N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing); N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase. N-Methylhydantoinase. Activity: 0.6-1.0 U/ mg. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: White lyophilizate. Source: E. coli. Species: Arthrobacter sp. N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing); N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase. Cat No: NATE-0904. | |
| sarcosine dehydrogenase | A flavoprotein (FMN). Tetrahydrofolate is also a substrate, being converted to N5,N10-methylenetetrahydrofolate. Group: Enzymes. Synonyms: sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine:(acceptor) oxidoreductase (demethylating). Enzyme Commission Number: EC 1.5.8.3. CAS No. 37228-65-2, 93389-49-2. 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-1562; sarcosine dehydrogenase; EC 1.5.8.3; 37228-65-2, 93389-49-2; sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine:(acceptor) oxidoreductase (demethylating). Cat No: EXWM-1562. | |
| N- (Dithiocarboxy) sarcosine, Diammonium Salt (DTCS) | A water soluble masking reagent for soft metal ions. When bound to FE2+, it is a hydrophillic spin trap for use in the study of nitric oxide. Group: Biochemicals. Alternative Names: DTCS. Grades: Highly Purified. Pack Sizes: 100mg. US Biological Life Sciences. |  Worldwide |
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