Modular organization of genes required for complex polyketide biosynthesis.Donadio S., Staver M.J., McAlpine J.B., Swanson S.J., Katz L.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNITCategoriesSequences, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCScience 252:675-679 (1991)Cited in3
6-deoxyerythronolide-B synthase 2 from Saccharopolyspora erythraea. Cloning of the structural gene, sequence analysis and inferred domain structure of the multifunctional enzyme.Bevitt D.J., Cortes J., Haydock S.F., Leadlay P.F.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNITStrainATCC 11635 / DSM 40517 / IFO 13426 / JCM 4026 / NCIB 8594CategoriesSequences, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 204:39-49 (1992)Cited in2
Identification of DEBS 1, DEBS 2 and DEBS 3, the multienzyme polypeptides of the erythromycin-producing polyketide synthase from Saccharopolyspora erythraea.Caffrey P., Bevitt D.J., Staunton J., Leadlay P.F.View abstractCited forPROTEIN SEQUENCE OF 2-12StrainCA340CategorySequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCFEBS Lett. 304:225-228 (1992)Cited in3
Structure and mechanism of the 6-deoxyerythronolide B synthase.Khosla C., Tang Y., Chen A.Y., Schnarr N.A., Cane D.E.View abstractCited forFUNCTION, PATHWAY, SUBUNITCategoriesFunction, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCAnnu. Rev. Biochem. 76:195-221 (2007)Cited in3
Prediction and manipulation of the stereochemistry of enoylreduction in modular polyketide synthases.Kwan D.H., Sun Y., Schulz F., Hong H., Popovic B., Sim-Stark J.C., Haydock S.F., Leadlay P.F.View abstractCited forFUNCTION, MUTAGENESIS OF TYR-2874, ACTIVE SITECategoriesFunction, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCChem. Biol. 15:1231-1240 (2008)Cited in1
Complete biosynthesis of erythromycin A and designed analogs using E. coli as a heterologous host.Zhang H., Wang Y., Wu J., Skalina K., Pfeifer B.A.View abstractCited forFUNCTION, CATALYTIC ACTIVITY, PATHWAYCategoryFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCChem. Biol. 17:1232-1240 (2010)Cited in3
Structural and functional analysis of C2-type ketoreductases from modular polyketide synthases.Zheng J., Keatinge-Clay A.T.View abstractCited forFUNCTION, MUTAGENESIS OF SER-1254 AND TYR-1267, DISRUPTION PHENOTYPE, REACTION MECHANISM, ACTIVE SITECategoriesFunction, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 410:105-117 (2011)Cited in2
The structure of docking domains in modular polyketide synthases.Broadhurst R.W., Nietlispach D., Wheatcroft M.P., Leadlay P.F., Weissman K.J.View abstractCited forSTRUCTURE BY NMR OF 3488-3547, SUBUNITCategoriesInteraction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCChem. Biol. 10:723-731 (2003)Cited in1Mapped to1
Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase.Tang Y., Chen A.Y., Kim C.Y., Cane D.E., Khosla C.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 27-922 IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, SUBSTRATE SPECIFICITY, ACTIVE SITE, COFACTOR, SUBUNITCategoriesFunction, Interaction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCChem. Biol. 14:931-943 (2007)Cited in1
Crystal structure of the erythromycin polyketide synthase dehydratase.Keatinge-Clay A.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2362-2653, FUNCTION, MUTAGENESIS OF ARG-2640, SUBUNIT, ACTIVE SITECategoriesFunction, Interaction, Phenotypes & Variants, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 384:941-953 (2008)Cited in1
Mapping the catalytic conformations of an assembly-line polyketide synthase module.Cogan D.P., Zhang K., Li X., Li S., Pintilie G.D., Roh S.H., Craik C.S., Chiu W., Khosla C.View abstractCategoryStructureSourcePDB: 7M7EPubMedEurope PMCScience 374:729-734 (2021)Cited in1Mapped to3
Modular polyketide synthase contains two reaction chambers that operate asynchronously.Bagde S.R., Mathews I.I., Fromme J.C., Kim C.Y.View abstractCategoryStructureSourcePDB: 7S6C, PDB: 7S6DPubMedEurope PMCScience 374:723-729 (2021)Cited in1Mapped to1
Structure-Function Analysis of the Extended Conformation of a Polyketide Synthase Module.Li X., Sevillano N., La Greca F., Deis L., Liu Y.C., Deller M.C., Mathews I.I., Matsui T., Cane D.E.[...], Khosla C.View abstractCategoryStructureSourcePDB: 6C9UPubMedEurope PMCJ Am Chem Soc 140:6518-6521 (2018)Mapped to1
Structure-based dissociation of a type I polyketide synthase module.Chen A.Y., Cane D.E., Khosla C.View abstractCategoryStructureSourcePDB: 2QO3PubMedEurope PMCChem Biol 14:784-792 (2007)Mapped to1
The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase.Tang Y., Kim C.Y., Mathews I.I., Cane D.E., Khosla C.View abstractCategoryStructureSourcePDB: 2QO3PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 103:11124-11129 (2006)Cited in1Mapped to1
Reconstituting modular activity from separated domains of 6- deoxyerythronolide B synthase.Kim C.Y., Alekseyev V.Y., Chen A.Y., Tang Y., Cane D.E., Khosla C.View abstractCategoryStructureSourcePDB: 2QO3PubMedEurope PMCBiochemistry 43:13892-13898 (2004)Mapped to2