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Enzyme Activity Measurement for Photinus-Luciferin 4-Monooxygenase (ATP-Hydrolysing)



For many years, Creative Enzymes has been conducting and developing a wide range of enzymatic assays used in multiple researches. By constantly striving for products of utmost quality, Creative Enzymes has earned the trust of countless customers, and is proud to offer highly sophisticated enzyme activity assay for photinus-luciferin 4-monooxygenase (ATP-hydrolysing).

Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) (EC 1.13.12.7), also known as photinus-luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing), is a peroxisomal protein found in the light-emitting organ within the abdomen of the firefly Photinus pyralis. This enzyme is the key in emitting flashes of light by firefly for attracting its mate. The molecular mass of this enzyme is about 62 kDa, but, unlike most other oxygenases, no redox prosthetic group is involved in the reaction catalyzed by photinus-luciferin 4-monooxygenase (ATP-hydrolysing). The structure of photinus-luciferin 4-monooxygenase (ATP-hydrolysing) from P. pyralis folds into two distinct domains, a large N-terminal domain comprising residues 4-436, and a C-terminal domain from residue 440 to 544. Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) catalyzes a multi-step reaction. In the first step, luciferin (compound I) reacts with Mg2+-ATP to form luciferyl adenylate (compound II) and pyrophosphate. The luciferyl adenylate is then oxidized by molecular oxygen, with the intermediate formation of the cyclic peroxide, a dioxetanone (compound III), and a molecule of AMP. The dioxetanone is decarboxylated as a result of intramolecular conversions (compound IV) to produce an electronically excited state of oxyluciferin in the enol or keto form (compound V).

Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) serves a critical role in molecular and cell biology, in particular for the efficient detection and quantification of ATP and as a reporter of genetic function. It has also been studied as a model for possible protein-anaesthetic interactions, being one of the few soluble proteins sensitive to a wide range of general anaesthetics. Moreover, the combined mutant luciferase, which has high luminescence intensity, is useful for detecting bacteria with high sensitivity in production safety tests. Thus, photinus-luciferin 4-monooxygenase (ATP-hydrolysing) plays a pivotal role in biotechnology, and the medical industry. The increasing number of studies on this enzyme necessitate the establish of accurate enzyme activity assays for this enzyme. With our professional team, Creative Enzymes promises to provide reliable tests on photinus-luciferin 4-monooxygenase (ATP-hydrolysing) activity measurement, using spectrophotometric assays. Unsurpassed by any others, Creative Enzymes provides innovative enzyme services with the most advanced instruments, and offers leading technical support and personalized customer service found nowhere else in the industry.

The crystal structure of firefly luciferase from P. pyralis. Figure: The crystal structure of firefly luciferase from P. pyralis.
PDB: 1LCI



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