Cytochrome P450 monooxygenase (CYP)

Short Description:

About CYP

ES-CYPs: A class of redox enzymes with mercaptan-heme as the active center to catalyze oxygen transfer. They are terminal oxygenases and needs heme to activate oxygen.

Cytochrome P450 monooxygenase catalyze the oxidation, epoxidation and hydroxylation of alkyl, hydroxylation and oxidation of ammonia, oxidation of sulfur, dealkylation(oxygen, sulfur, ammonia), oxidative dehydrogenation, deamination and dehalogenation.
There are 8 kinds of cytochrome P450 monooxygenase products (Number as ES-CYP-101~ES-CYP-108) developed by SyncoZymes.

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Product Detail

Product Tags

About CYP:

Catalytic reaction type:


Product Information:

Enzymes Screening Kit (SynKit) Specification
Enzyme Powder ES-CYP-101~ ES-CYP-108 a set of 8 Cytochrome P450 Monooxygenases, 50 mg each 8 items * 50mg / item, or other quantity
Screening Kit (SynKit) ES-CYP-800 a set of 8 Cytochrome P450 Monooxygenases,1mg each 8 items * 1mg / item


★ Broad substrate spectrum.
★ High conversion.
★ Less by-products.
★ Mild reaction conditions.
★ Environmentally friendly.

Instructions for use:

➢ Normally, the reaction system should include substrate, buffer solution (The optimum reaction pH of enzyme), coenzyme (NAD(H) or NADP(H)), coenzyme regeneration system (e.g. glucose and glucose dehydrogenase) and the ES-CYP. coenzyme and coenzyme regeneration system could be replaced by hydrogen peroxide in partial reaction system.
➢ All kinds of ES-CYPs corresponding to various optimum reaction conditions should be studied individually.
➢ High concentration Substrate or product with may inhibit ES-CYP’s activity. However, the inhibition can be relieved by batch addition of substrate.

Application Examples:

Example 1 (1):


Example 2 (2):


Example 3 (3):


Example 4(4):



Keep 2 years below -20℃.


Never contact with extreme conditions such as: high temperature, high/low pH and high concentration organic solvent.


1. Zaretzki J, Matlock M, and Swamidass S J. J. Chem. Inf. Model, 2013, 53, 3373–3383.
2. Gannett P M., Kabulski J,  Perez F A., e tal. J. Am. Chem. Soc., 2006, 128 (26),  8374–8375.
3. Cryle M J.,  Matovic N J., and  De Voss J J. Org. Lett., 2003, 5 (18), 3341–3344.
4. Kawauchi, H., Sasaki, J., Adachi, T., e tal. Biochim. Biophys. Acta, 1994, 1219, 179.
5. Yasutake, Y., Fujii, Y.; Cheon, W. K. e tal. Acta Crystallogr. 2009, 65, 372.

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