Divergence of multimodular polyketide synthases revealed by a didomain structure - Test2 - elhamkhani - TriplyDB

Divergence of multimodular polyketide synthases revealed by a didomain structure

Divergence of multimodular polyketide synthases revealed by a didomain structure

http://www.wikidata.org/entity/Q27679312

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The Missing Linker: A Dimerization Motif Located within Polyketide Synthase Modules Structural and Stereochemical Analysis of a Modular Polyketide Synthase Ketoreductase Domain Required for the Generation of a cis-Alkene The use of ene adducts to study and engineer enoyl-thioester reductases Domain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferase Architecture of the polyketide synthase module: surprises from electron cryo-microscopy Recent advances in the elucidation of enzymatic function in natural product biosynthesis Architectures of whole-module and bimodular proteins from the 6-deoxyerythronolide B synthase Polyketide intermediate mimics as probes for revealing cryptic stereochemistry of ketoreductase domains.Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase Methyltransferases excised from trans-AT polyketide synthases operate on N-acetylcysteamine-bound substrates.Structural analysis of protein-protein interactions in type I polyketide synthases Polyketide stereocontrol: a study in chemical biology.The structures of type I polyketide synthases.Dissecting complex polyketide biosynthesis.Uncovering the structures of modular polyketide synthases.Stereocontrol within polyketide assembly lines.The structural biology of biosynthetic megaenzymes.Genetic engineering of modular PKSs: from combinatorial biosynthesis to synthetic biology.Structure and mechanism of assembly line polyketide synthases.Structure of a modular polyketide synthase.The Structural Relationship between Iterative and Modular PKSs.Substrate selectivity of an isolated enoyl reductase catalytic domain from an iterative highly reducing fungal polyketide synthase reveals key components of programming.Tylosin polyketide synthase module 3: stereospecificity, stereoselectivity and steady-state kinetic analysis of β-processing domains via diffusible, synthetic substrates.Identification of novel protein domains required for the expression of an active dehydratase fragment from a polyunsaturated fatty acid synthase.ClusterCAD: a computational platform for type I modular polyketide synthase design.Engineered polyketides: Synergy between protein and host level engineering.Insights into the programmed ketoreduction of partially reducing polyketide synthases: stereo- and substrate-specificity of the ketoreductase domain

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P2860

Divergence of multimodular polyketide synthases revealed by a didomain structure

http://www.wikidata.org/entity/Q27679312

description

2012 nî lūn-bûn

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2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2012年の論文

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2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Divergence of multimodular polyketide synthases revealed by a didomain structure

@ast

Divergence of multimodular polyketide synthases revealed by a didomain structure

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Divergence of multimodular polyketide synthases revealed by a didomain structure

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type

label

Divergence of multimodular polyketide synthases revealed by a didomain structure

@ast

Divergence of multimodular polyketide synthases revealed by a didomain structure

@en

Divergence of multimodular polyketide synthases revealed by a didomain structure

@nl

prefLabel

Divergence of multimodular polyketide synthases revealed by a didomain structure

@ast

Divergence of multimodular polyketide synthases revealed by a didomain structure

@en

Divergence of multimodular polyketide synthases revealed by a didomain structure

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Nature Chemical Biology

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Divergence of multimodular polyketide synthases revealed by a didomain structure

@en

P2093

Adrian T Keatinge-Clay

http://www.w3.org/2001/XMLSchema#string

Darren C Gay

http://www.w3.org/2001/XMLSchema#string

Jianting Zheng

http://www.w3.org/2001/XMLSchema#string

Mark A White

http://www.w3.org/2001/XMLSchema#string

P2860

Medium- and short-chain dehydrogenase/reductase gene and protein families : the MDR superfamily

3D domain swapping: as domains continue to swap

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: Versatility from a unique substrate channel

Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance

Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers

A tylosin ketoreductase reveals how chirality is determined in polyketides

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

Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties

The crystal structure of a mammalian fatty acid synthase

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scholarly article

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4773293

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10.1038/NCHEMBIO.964

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7

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8

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Borries Demeler

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2012-07-01T00:00:00Z

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225064050

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1053513340

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22634636

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3477503

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