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Exploring nicotinamide cofactor promiscuity in NAD(P)H-dependent flavin containing monooxygenases (FMOs) using natural variation within the phosphate binding loop. Structure and activity of FMOs from Cellvibrio sp. BR and Pseudomonas stutzeri NF13
Flavin-containing monooxygenases (FMOs) catalyse asymmetric oxidation reactions that have potential for preparative organic synthesis, but most use the more expensive, phosphorylated nicotinamide cofactor NADPH to reduce FAD to FADH(2) prior to formation of the (hydro)peroxy intermediate required fo...
Uloženo v:
| Vydáno v: | J Mol Catal B Enzym |
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| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Elsevier Science
2014
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4220118/ https://ncbi.nlm.nih.gov/pubmed/25383040 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcatb.2014.08.019 |
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