Erythronolide synthase (original) (raw)

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In enzymology, an erythronolide synthase (also 6-Deoxyerythronolide B Synthase or DEBS) is an enzyme that catalyzes the chemical reaction 6 malonyl-CoA + propanoyl-CoA 7 CoA + 6-deoxyerythronolide B Thus, the two substrates of this enzyme are malonyl-CoA and propanoyl-CoA, whereas its two products are CoA and . This enzyme participates in .

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dbo:abstract In enzymology, an erythronolide synthase (also 6-Deoxyerythronolide B Synthase or DEBS) is an enzyme that catalyzes the chemical reaction 6 malonyl-CoA + propanoyl-CoA 7 CoA + 6-deoxyerythronolide B Thus, the two substrates of this enzyme are malonyl-CoA and propanoyl-CoA, whereas its two products are CoA and . This enzyme participates in . This enzyme belongs to the family of transferases, it has been identified as part of a Type 1 polyketide synthase module. DEBS is found in Saccharopolyspora erythraea and other actinobacteria, and is 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. (en) La eritronolide sintasi è un enzima appartenente alla classe delle transferasi, che catalizza la seguente reazione: 6 malonil-CoA + ⇄ 7 CoA + 6-deossi B Il prodotto, che contiene un anello lattone a 14 membri, è un intermedio nella biosintesi degli antibiotici della famiglia dell'eritromicina. La biosintesi della 6-deossieritronolide B richiede la presenza di 28 siti attivi disposti esattamente lungo tre polipeptidi definiti DEBS-1, -2 e -3. Il prodotto polichetidico è sintetizzto dall'azione successiva di un doppio dominio di caricamento, da sei moduli di estensione e da un dominio tioesterasico terminale. Ogni modulo di estensione contiene attività chetosintasica (KS), aciltransferasica (AT) ed una proteina trasportante acili (ACP). Il dominio KS è sia in grado di accettare dal precedente modulo la catena polichetidica in accrescimento, sia catalizzare la seguente condensazione decarbossilativa tra il substrato e l'unità di estensione contenente un residuo metilmalonile legato ad ACP. Questa attività combinata porta alla produzione di un nuovo intermedio polichetidico esteso di due atomi di carbonio. (it)
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rdfs:comment In enzymology, an erythronolide synthase (also 6-Deoxyerythronolide B Synthase or DEBS) is an enzyme that catalyzes the chemical reaction 6 malonyl-CoA + propanoyl-CoA 7 CoA + 6-deoxyerythronolide B Thus, the two substrates of this enzyme are malonyl-CoA and propanoyl-CoA, whereas its two products are CoA and . This enzyme participates in . (en) La eritronolide sintasi è un enzima appartenente alla classe delle transferasi, che catalizza la seguente reazione: 6 malonil-CoA + ⇄ 7 CoA + 6-deossi B Il prodotto, che contiene un anello lattone a 14 membri, è un intermedio nella biosintesi degli antibiotici della famiglia dell'eritromicina. La biosintesi della 6-deossieritronolide B richiede la presenza di 28 siti attivi disposti esattamente lungo tre polipeptidi definiti DEBS-1, -2 e -3. Il prodotto polichetidico è sintetizzto dall'azione successiva di un doppio dominio di caricamento, da sei moduli di estensione e da un dominio tioesterasico terminale. Ogni modulo di estensione contiene attività chetosintasica (KS), aciltransferasica (AT) ed una proteina trasportante acili (ACP). Il dominio KS è sia in grado di accettare dal preceden (it)
rdfs:label Erythronolide synthase (en) Eritronolide sintasi (it)
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