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Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Arthrobacter sp. can also act on 3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf. EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase), but more slowly. Group: Enzymes. Synonyms: (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase. Enzyme Commission Number: EC 1.13.11.48. CAS No. 160995-63-1. 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-0566; 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase; EC 1.13.11.48; 160995-63-1; (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase. Cat No: EXWM-0566.
3-hydroxy-4-oxoquinoline 2,4-dioxygenase
Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Pseudomonas putida is highly specific for this substrate. Group: Enzymes. Synonyms: (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase; 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase; 3-hydroxy-4(1H)-one, 2,4-dioxygenase; quinoline-3,4-diol 2,4-dioxygenase. Enzyme Commission Number: EC 1.13.11.47. CAS No. 238093-32-8. 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-0565; 3-hydroxy-4-oxoquinoline 2,4-dioxygenase; EC 1.13.11.47; 238093-32-8; (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase; 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase; 3-hydroxy-4(1H)-one, 2,4-dioxygenase; quinoline-3,4-diol 2,4-dioxygenase. Cat No: EXWM-0565.
5-methyltetrahydrofolate: corrinoid/iron-sulfur protein Co-methyltransferase
Catalyses the transfer of a methyl group from the N5 group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea. Group: Enzymes. Synonyms: acsE (gene name). Enzyme Commission Number: EC 2.1.1.258. 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-1862; 5-methyltetrahydrofolate: corrinoid/iron-sulfur protein Co-methyltransferase; EC 2.1.1.258; acsE (gene name). Cat No: EXWM-1862.
5-methyltetrahydrosarcinapterin: corrinoid/iron-sulfur protein Co-methyltransferase
Catalyses the transfer of a methyl group from the cobamide cofactor of a corrinoid/Fe-S protein to the N5 group of tetrahydrosarcinapterin. Forms, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, the acetyl-CoA decarbonylase/synthase complex that catalyses the demethylation of acetyl-CoA in a reaction that also forms CO2. This reaction is a key step in methanogenesis from acetate. Group: Enzymes. Synonyms: cdhD (gene name); cdhE (gene name). Enzyme Commission Number: EC 2.1.1.245. 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-1848; 5-methyltetrahydrosarcinapterin: corrinoid/iron-sulfur protein Co-methyltransferase; EC 2.1.1.245; cdhD (gene name); cdhE (gene name). Cat No: EXWM-1848.
abieta-7,13-diene hydroxylase
A heme-thiolate protein (P-450). This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine). The enzyme is localized in the microsomal fraction and requires both oxygen and NADPH. Inhibition by carbon monoxide and several substituted N-heterocyclic inhibitors suggests that the enzyme is a cytochrome P-450-dependent monooxygenase. Activity is induced by wounding of the plant tissue. Group: Enzymes. Synonyms: abietadiene hydroxylase (ambiguous). Enzyme Commission Number: EC 1.14.13.108. 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-0707; abieta-7,13-diene hydroxylase; EC 1.14.13.108; abietadiene hydroxylase (ambiguous). Cat No: EXWM-0707.
aerobic carbon monoxide dehydrogenase
This enzyme, found in carboxydotrophic bacteria, catalyses the oxidation of CO to CO2 under aerobic conditions. The enzyme contains a binuclear Mo-Cu cluster in which the copper is ligated to a molybdopterin center via a sulfur bridge. The enzyme also contains two [2Fe-2S] clusters and FAD, and belongs to the xanthine oxidoreductase family. The CO2 that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor. cf. EC 1.2.7.4, anaerobic carbon monoxide dehydrogenase. Group: Enzymes. Synonyms: MoCu-CODH; coxSML (gene names); molybdoenzyme carbon monoxide dehydrogenase. Enzyme Commission Number: EC 1.2.5.3. 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-1222; aerobic carbon monoxide dehydrogenase; EC 1.2.5.3; MoCu-CODH; coxSML (gene names); molybdoenzyme carbon monoxide dehydrogenase. Cat No: EXWM-1222.
anaerobic carbon-monoxide dehydrogenase
This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [...-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase. Group: Enzymes. Synonyms: Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Enzyme Commission Number: EC 1.2.7.4. 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-1227; anaerobic carbon-monoxide dehydrogenase; EC 1.2.7.4; Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Cat No: EXWM-1227.
carbon-monoxide dehydrogenase (cytochrome b-561)
Contains molybdopterin cytosine dinucleotide, FAD and [2Fe-2S]-clusters. Oxygen, methylene blue and iodonitrotetrazolium chloride can act as nonphysiological electron acceptors. Group: Enzymes. Synonyms: carbon monoxide oxidase; carbon monoxide oxygenase (cytochrome b-561); carbon monoxide:methylene blue oxidoreductase; CO dehydrogenase; carbon-monoxide dehydrogenase. Enzyme Commission Number: EC 1.2.2.4. CAS No. 395639-79-9. 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-1205; carbon-monoxide dehydrogenase (cytochrome b-561); EC 1.2.2.4; 395639-79-9; carbon monoxide oxidase; carbon monoxide oxygenase (cytochrome b-561); carbon monoxide:methylene blue oxidoreductase; CO dehydrogenase; carbon-monoxide dehydrogenase. Cat No: EXWM-1205.
CO-methylating acetyl-CoA synthase
Contains nickel, copper and iron-sulfur clusters. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin), in the synthesis of acetyl-CoA from CO2 and H2. Group: Enzymes. Enzyme Commission Number: EC 2.3.1.169. CAS No. 176591-19-8. 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-2109; CO-methylating acetyl-CoA synthase; EC 2.3.1.169; 176591-19-8. Cat No: EXWM-2109.
Cystathionine gamma-lyase, Recombinant
Cystathionine gamma-lyase (CGL),or cystathionase (CSE, EC 4.4.1.1) , the enzyme participating in the synthesis of cysteine, catalyzes cystathionine deamination action, and form cysteine, alpha ketone butyric acid and NH3. In some bacteria and mammals, including humans, this enzyme takes part in generating hydrogen sulfide. Hydrogen sulfide is one of a few gases that was recently discovered to have arole in cell signaling in the body. As a new gaseous signal molecular, h2s has the similar but different mechanisms with carbon monoxide (co), nitric oxide (no) in diastolic function forblood vessels, which has several function such as the proliferation of vascular smooth muscle...e; CGL; cystathionase; CSE; EC 4.4.1.1; homoserine deaminase; homoserine dehydratase; cystine desulfhydrase; cysteine desulfhydrase; γ-cystathionase; cystathionase; homoserine deaminase-cystathionase; γ-CTL; cystalysin; cysteine lyase; L-cystathionine cysteine-lyase (deaminating); cystathionine γ-lyase. Enzyme Commission Number: EC 4.4.1.1. Purity: >90% (SDS-PAGE test). Mole weight: About 44kDa (SDS-PAGE detection). Activity: 11.25 KU/mg protein. Appearance: Yellowish liquid (or lyophilized powder). Storage: 4°C, store at -20°C for long-term preservation. Form: Freeze dried powder. Cystathionine gamma-lyase; CGL; cystathionase; CSE; EC 4.4.1.1; homoserine
oxalate oxidoreductase
Contains thiamine diphosphate and [4Fe-4S] clusters. Acceptors include ferredoxin and the nickel-dependent carbon monoxide dehydrogenase (EC 1.2.7.4). Group: Enzymes. Enzyme Commission Number: EC 1.2.7.10. 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-1224; oxalate oxidoreductase; EC 1.2.7.10. Cat No: EXWM-1224.
Zinc (II) Protoporphyrin IX - CAS 15442-64-5
A potent and selective inhibitor of heme oxygenase, the enzyme which generates carbon monoxide (CO) and biliverdin. Group: Fluorescence/luminescence spectroscopy.
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