Structure, catalysis, and inhibition mechanism of prenyltransferase
العنوان: | Structure, catalysis, and inhibition mechanism of prenyltransferase |
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المؤلفون: | Hsin Yang Chang, Tien Hsing Cheng, Andrew H.-J. Wang |
المصدر: | Iubmb Life |
بيانات النشر: | John Wiley & Sons, Inc., 2020. |
سنة النشر: | 2020 |
مصطلحات موضوعية: | 0301 basic medicine, Protein Conformation, medicine.medical_treatment, Clinical Biochemistry, Prenyltransferase, Biochemistry, Cyclase, Catalysis, Steroid, Terpene, 03 medical and health sciences, 0302 clinical medicine, Prenylation, Genetics, medicine, Animals, Humans, Enzyme Inhibitors, Molecular Biology, Critical Reviews, terpene, ATP synthase, biology, isoprenoid, Chemistry, organic chemicals, Critical Review, farnesyl diphosphate, Cell Biology, Dimethylallyltranstransferase, Terpenoid, 030104 developmental biology, 030220 oncology & carcinogenesis, biology.protein, prenyltransferase, Protein prenylation, lipids (amino acids, peptides, and proteins), terpenoid |
الوصف: | Isoprenoids, also known as terpenes or terpenoids, represent a large family of natural products composed of five‐carbon isopentenyl diphosphate or its isomer dimethylallyl diphosphate as the building blocks. Isoprenoids are structurally and functionally diverse and include dolichols, steroid hormones, carotenoids, retinoids, aromatic metabolites, the isoprenoid side‐chain of ubiquinone, and isoprenoid attached signaling proteins. Productions of isoprenoids are catalyzed by a group of enzymes known as prenyltransferases, such as farnesyltransferases, geranylgeranyltransferases, terpenoid cyclase, squalene synthase, aromatic prenyltransferase, and cis‐ and trans‐prenyltransferases. Because these enzymes are key in cellular processes and metabolic pathways, they are expected to be potential targets in new drug discovery. In this review, six distinct subsets of characterized prenyltransferases are structurally and mechanistically classified, including (1) head‐to‐tail prenyl synthase, (2) head‐to‐head prenyl synthase, (3) head‐to‐middle prenyl synthase, (4) terpenoid cyclase, (5) aromatic prenyltransferase, and (6) protein prenylation. Inhibitors of those enzymes for potential therapies against several diseases are discussed. Lastly, recent results on the structures of integral membrane enzyme, undecaprenyl pyrophosphate phosphatase, are also discussed. |
اللغة: | English |
تدمد: | 1521-6551 1521-6543 |
الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bb2a5c3a42f2e738d23e16011be88f4Test http://europepmc.org/articles/PMC7839719Test |
حقوق: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....7bb2a5c3a42f2e738d23e16011be88f4 |
قاعدة البيانات: | OpenAIRE |
تدمد: | 15216551 15216543 |
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