The biochemical basis for stereochemical control in polyketide biosynthesis. - Wikidata - awgldk - TriplyDB

The biochemical basis for stereochemical control in polyketide biosynthesis.

The biochemical basis for stereochemical control in polyketide biosynthesis.

http://www.wikidata.org/entity/Q41275766

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Structural and Biochemical Analyses of Regio- and Stereospecificities Observed in a Type II Polyketide Ketoreductase Structural Studies of an A2-Type Modular Polyketide Synthase Ketoreductase Reveal Features Controlling α-Substituent Stereochemistry Structural and Stereochemical Analysis of a Modular Polyketide Synthase Ketoreductase Domain Required for the Generation of a cis-Alkene Divergence of multimodular polyketide synthases revealed by a didomain structure Structure and Stereospecificity of the Dehydratase Domain from the Terminal Module of the Rifamycin Polyketide Synthase A labile point in mutant amphotericin polyketide synthases Elucidation of the cryptic epimerase activity of redox-inactive ketoreductase domains from modular polyketide synthases by tandem equilibrium isotope exchange SBSPKS: structure based sequence analysis of polyketide synthases Programming of erythromycin biosynthesis by a modular polyketide synthase Polyketide intermediate mimics as probes for revealing cryptic stereochemistry of ketoreductase domains.Essential role of the donor acyl carrier protein in stereoselective chain translocation to a fully reducing module of the nanchangmycin polyketide synthase Epigenetic genome mining of an endophytic fungus leads to the pleiotropic biosynthesis of natural products Reprogramming a module of the 6-deoxyerythronolide B synthase for iterative chain elongation.Epimerase and Reductase Activities of Polyketide Synthase Ketoreductase Domains Utilize the Same Conserved Tyrosine and Serine Residues.Stereochemistry of reductions catalyzed by methyl-epimerizing ketoreductase domains of polyketide synthases.Structural analysis of protein-protein interactions in type I polyketide synthases Coupled methyl group epimerization and reduction by polyketide synthase ketoreductase domains. Ketoreductase-catalyzed equilibrium isotope exchange.Polyketide stereocontrol: a study in chemical biology.Investigating the reactivities of a polyketide synthase module through fluorescent click chemistry.The structures of type I polyketide synthases.Dissecting complex polyketide biosynthesis.Assembly line polyketide synthases: mechanistic insights and unsolved problems.Stereocontrol within polyketide assembly lines.Genetic engineering of modular PKSs: from combinatorial biosynthesis to synthetic biology.Polyene macrolide biosynthesis in streptomycetes and related bacteria: recent advances from genome sequencing and experimental studies.Navigating the fungal polyketide chemical space: from genes to molecules.A fungal ketoreductase domain that displays substrate-dependent stereospecificity.Stereospecificity of the dehydratase domain of the erythromycin polyketide synthase.A trans-acting ketoreductase in biosynthesis of a symmetric polyketide dimer SIA7248.Elucidation of the Stereospecificity of C-Methyltransferases from trans-AT Polyketide Synthases.Configurational assignment of secondary hydroxyl groups and methyl branches in polyketide natural products through bioinformatic analysis of the ketoreductase domain.Elucidation of the Cryptic Methyl Group Epimerase Activity of Dehydratase Domains from Modular Polyketide Synthases Using a Tandem Modules Epimerase Assay.Mechanism and Stereochemistry of Polyketide Chain Elongation and Methyl Group Epimerization in Polyether Biosynthesis.Engineered polyketides: Synergy between protein and host level engineering.Synthesis of ent-BE-43547A1 reveals a potent hypoxia-selective anticancer agent and uncovers the biosynthetic origin of the APD-CLD natural products.Evaluating Ketoreductase Exchanges as a Means of Rationally Altering Polyketide Stereochemistry.Insights into the stereospecificity of ketoreduction in a modular polyketide synthase.In vivo trapping of polyketide intermediates from an assembly line synthase using malonyl carba(dethia)-N-acetyl cysteamines.Substrate-dependent stereospecificity of Tyl-KR1: an isolated polyketide synthase ketoreductase domain from Streptomyces fradiae.Substrate-bound structures of a ketoreductase from amphotericin modular polyketide synthase.

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P2860

The biochemical basis for stereochemical control in polyketide biosynthesis.

http://www.wikidata.org/entity/Q41275766

description

2009 nî lūn-bûn

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

@zh-tw

2009年论文

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2009年论文

@zh

2009年论文

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name

The biochemical basis for stereochemical control in polyketide biosynthesis.

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type

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The biochemical basis for stereochemical control in polyketide biosynthesis.

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The biochemical basis for stereochemical control in polyketide biosynthesis.

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Journal of the American Chemical Society

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The biochemical basis for stereochemical control in polyketide biosynthesis.

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Alice Y Chen

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Chaitan Khosla

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Chiara R Valenzano

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David E Cane

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Rachel J Lawson

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P2860

The structure of docking domains in modular polyketide synthases

A tylosin ketoreductase reveals how chirality is determined in polyketides

Structural and Mechanistic Analysis of Protein Interactions in Module 3 of the 6-Deoxyerythronolide B Synthase

Solution structure and proposed domain-domain recognition interface of an acyl carrier protein domain from a modular polyketide synthase

Crystal Structure of the Erythromycin Polyketide Synthase Dehydratase

Tolerance and specificity of polyketide synthases

Ketoreduction in mycolactone biosynthesis: insight into substrate specificity and stereocontrol from studies of discrete ketoreductase domains in vitro

Post-translational modification of polyketide and nonribosomal peptide synthases

Spontaneous α-N-6-Phosphogluconoylation of a “His Tag” inEscherichia coli:The Cause of Extra Mass of 258 or 178 Da in Fusion Proteins

Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis.

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10.1021/JA908296M

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51

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19928853

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3699857

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