CAS 9001-96-1|Pyruvate Oxidase
| Common Name | Pyruvate Oxidase | ||
|---|---|---|---|
| CAS Number | 9001-96-1 | Molecular Weight | / |
| Density | / | Boiling Point | / |
| Molecular Formula | / | Melting Point | / |
| MSDS | USA | Flash Point | / |
Names
| Name | PYRUVATE OXIDASE |
|---|---|
| Synonym | More Synonyms |
Pyruvate Oxidase BiologicalActivity
| Description | Pyruvate oxidase (PoxB) is a thiamine pyrophosphate-dependent oxidase that catalyzes the oxidative decarboxylation of pyruvate to acetyl phosphate, carbon dioxide and water. Pyruvate oxidase is an important enzyme in bacterial metabolism and is often used in biochemical research[1]. |
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| Related Catalog | Research Areas >>Others |
| References | [1]. Louis P Cornacchione, et al. Hydrogen peroxide-producing pyruvate oxidase from Lactobacillus delbrueckii is catalytically activated by phosphotidylethanolamine. BMC Microbiol. 2020 May 24;20(1):128. |
Chemical & Physical Properties
| Storage condition | −20°C |
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Safety Information
| Personal Protective Equipment | Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter |
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| Safety Phrases | 24/25 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | 3 |
Articles33
More Articles| Alternating sites reactivity is a common feature of thiamin diphosphate-dependent enzymes as evidenced by isothermal titration calorimetry studies of substrate binding. Biochemistry 52(15) , 2505-7, (2013) Thiamin diphosphate (ThDP)-dependent enzymes play vital roles in cellular metabolism in all kingdoms of life. In previous kinetic and structural studies, a communication between the active centers in ... | |
| A luminol chemiluminescence method for sensing histidine and lysine using enzyme reactions. Anal. Biochem. 443(1) , 22-6, (2013) The analysis of free amino acids in urine and plasma is useful for estimating disease status in clinical diagnoses. Changes in the concentration of free amino acids in foods are also useful markers of... | |
| Using substrate analogues to probe the kinetic mechanism and active site of Escherichia coli MenD. Biochemistry 50(40) , 8712-21, (2011) MenD catalyzes the thiamin diphosphate-dependent decarboxylative carboligation of α-ketoglutarate and isochorismate. The enzyme is essential for menaquinone biosynthesis in many bacteria and has been ... |
Synonyms
| EINECS 232-644-5 |
