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propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
6 methylmalonyl-CoA + propionyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide b + 7 CoA + 6 CO2 + H2O + 6 NADP+
propanoyl-CoA + (2S)-methylmalonyl-CoA + NADPH
(3R,4S,5R,6R)-6-ethyl-4-hydroxy-3,5-dimethyloxan-2-one + ?
-
-
-
?
propanoyl-CoA + 5 (2S)-methylmalonyl-CoA + (2S)-ethylmalonyl-CoA + 6 NADPH + 6 H+
(3R,4S,5R,6R)-6-ethyl-4-hydroxy-3,5-dimethyltetrahydro-2H-pyran-2-one + ?
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product of truncated enzyme consisting of loading didomain-module1-module2+thioesterase
-
?
propanoyl-CoA + 5 (2S)-methylmalonyl-CoA + (2S)-ethylmalonyl-CoA + 6 NADPH + 6 H+
(3R,5R,6S)-6-[(2S,3R)-3-hydroxypentan-2-yl]-3,5-dimethyldihydro-2H-pyran-2,4(3H)-dione + ?
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product of truncated enzyme consisting of loading didomain-module1-module2-module3+thioesterase
-
?
propanoyl-CoA + 5 (2S)-methylmalonyl-CoA + (2S)-ethylmalonyl-CoA + 6 NADPH + 6 H+
8-ethyl-8-desmethyl-6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
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putative analog, 8-ethyl-8-desmethyl-6-deoxyerythronolide B, is generated by the assembly line in the presence of non-limiting concentrations of ethylmalonyl-CoA and is produced in comparable amounts to the natural 6-dEB product
-
?
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
additional information
?
-
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
-
-
-
?
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
-
-
-
?
6 methylmalonyl-CoA + propionyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide b + 7 CoA + 6 CO2 + H2O + 6 NADP+
-
-
-
?
6 methylmalonyl-CoA + propionyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide b + 7 CoA + 6 CO2 + H2O + 6 NADP+
-
formation of a key intermediate in the biosynthesis of erythromycin
-
?
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
-
-
-
-
?
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
-
-
-
?
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
-
-
-
?
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+
6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
-
-
-
?
additional information
?
-
-
unidirectional translocation of the growing polyketide chain along the 6-deoxyerythronolide B synthase, ratchet mechanism, overview
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-
?
additional information
?
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the cis-acyltransferase domain from DEBS module 3 transfers a methylmalonyl extender unit from the corresponding carboxyacyl-CoA precursor onto the phosphopantetheine arm of the acyl carrier protein within the same module. The presence of the acyl carrier protein has little effect on the specificity of the cis-acyltransferase domain for carboxyacyl-CoA substrates, but has a marked influence on the corresponding specificity parameters for the trans-acyltransferases from the disorazole and kirromycin synthases. Comparative analysis of the substrate specificity
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?
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?
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x * 37000, enzyme may be a component of a multifunctional protein or may exist as a dimer SDS-PAGE
homodimer
thioesterase domain, 2 * 33000
oligomer
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the polyketide product is synthesized by the processive action of a loading didomain, six extension modules and a terminal thioesterase domain, as a minimal requirement for chain extension, each module contains a set of three functional domains, a ketosynthase, an acyltransferae, and an acyl carrier protein
additional information
DEBS is organized into modules comprising of multiple catalytic domains, to assemble short acyl-CoA precursors into complex polyketide products, each module contains minimally three functional domains, a beta-ketosynthase, an acyltransferase, and an acyl carrier protein
additional information
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DEBS is organized into modules comprising of multiple catalytic domains, to assemble short acyl-CoA precursors into complex polyketide products, each module contains minimally three functional domains, a beta-ketosynthase, KS, an acyltransferase, AT, and an acyl carrier protein, ACP
additional information
deoxyerythronolide B synthase consists of several modules, formed by acyltransferases, acyl carrier proteins, ketosynthases, ketoreductases, dehydratases, enoylreductases and thioesterases
additional information
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solution structure of ACP2, the tertiary fold of ACP2 is a three-helix bundle, overview
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Roberts, G.; Leadly, P.F.
Use of [3H]tetrahydrocerulenin to assay condensing enzyme activity in Streptomyces erythreus
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12
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Saccharopolyspora erythraea
-
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Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: Versatility from a unique substrate channel
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98
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Saccharopolyspora erythraea (Q03133)
brenda
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Biosynthesis of complex polyketides in a metabolically engieered strain of Escherichia coli
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20
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Dunn, B.J.; Watts, K.R.; Robbins, T.; Cane, D.E.; Khosla, C.
Comparative analysis of the substrate specificity of trans- versus cis-acyltransferases of assembly line polyketide synthases
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53
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brenda
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Towards a characterization of the structural determinants of specificity in the macrocyclizing thioesterase for deoxyerythronolide B biosynthesis
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2016
Saccharopolyspora erythraea (Q03133)
brenda
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In vitro reconstitution and analysis of the 6-deoxyerythronolide B synthase
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Architectures of whole-module and bimodular proteins from the 6-deoxyerythronolide B synthase
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Inversion of extender unit selectivity in the erythromycin polyketide synthase by acyltransferase domain engineering
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12
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Roles of conserved active site residues in the ketosynthase domain of an assembly line polyketide synthase
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2016
Saccharopolyspora erythraea (Q03131 and Q03132 and Q03133)
brenda
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Saccharopolyspora erythraea (Q03131 and Q03132 and Q03133)
brenda