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| DEBS (6-deoxyerythronolide B synthase) ： ウィキペディア英語版 |
6-Deoxyerythronolide B synthase
6-Deoxyerythronolide B Synthase or DEBS has been identified as a Type 1 polyketide synthase. DEBS is found in ''Saccharopolyspora erythraea'' and responsible for the synthesis of the macrolide ring which is the precursor of the antibiotic erythromycin. There have been three categories of polyketide synthases identified to date, type 1, 2 and 3. Type one synthases involve large multidomain proteins containing all the sites necessary for polyketide synthesis. Type two synthases contain active sites distributed among several smaller polypeptides, and type three synthases are large multi-protein complexes containing modules which have a single active site for each and every step of polyketide synthesis. In the case of DEBS, there are three large multi-functional proteins, DEBS 1,2, and 3, that each exist as a dimer of two modules. Each module consists of a minimum of a Ketosynthase (KS), Acyl carrier protein (ACP) site, and acyltransferase (AT), but may also contain a Ketoreductase (KR), Dehydrotase (DH), and Enol Reductase (ER) for additional reduction reactions. The DEBS complex also contains a Loading Domain on module 1 consisting of an acyl carrier protein and an acyltransferase. The terminal Thioesterase acts solely to terminate DEBS polyketide synthesis and cyclize the macrolide ring.〔Khosla, C., Tang, Y., Chen, A. Y., Schnarr, N. A., and Cane, D. E. (2007). Structure and Mechanism of the 6-Deoxyerythronolide B Synthase. Annual Review of Biochemistry, 76,195–221〕〔Staunton, J. and Weissman, K. J. (2001). Polyketide biosynthesis: a millennium review. The Royal Society of Chemistry, 18, 380–416〕〔Katz, L. (2009). The DEBS Paradigm for Type I Modular Polyketide Synthases and Beyond. Methods in Enzymology, 459, 113-142〕
== Module components and functions ==
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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