Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis - Wikidata - awgldk - TriplyDB

Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis

Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis

http://www.wikidata.org/entity/Q27639897

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The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU Structural basis for recruitment of tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation Structural Basis for the Activity and Substrate Specificity of Fluoroacetyl-CoA Thioesterase FlK Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics High resolution crystal structure of Clostridium propionicum β-alanyl-CoA:ammonia lyase, a new member of the "hot dog fold" protein superfamily The missing piece of the type II fatty acid synthase system from Mycobacterium tuberculosis Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis Revisiting the assignment of Rv0241c to fatty acid synthase type II of Mycobacterium tuberculosis Synthetic biology approaches to fluorinated polyketides Analysis of proteins with the 'hot dog' fold: prediction of function and identification of catalytic residues of hypothetical proteins.Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli.A distinct MaoC-like enoyl-CoA hydratase architecture mediates cholesterol catabolism in Mycobacterium tuberculosis.Polyester synthases: natural catalysts for plastics.Contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp.Catalytic control of enzymatic fluorine specificity Active site comparisons and catalytic mechanisms of the hot dog superfamily.Enoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei.Extension of the classical classification of β-turns.Molecular recognition of fluorine impacts substrate selectivity in the fluoroacetyl-CoA thioesterase FlK.Crystallization and preliminary X-ray analysis of the MaoC-like dehydratase from Phytophthora capsici.Alteration of chain length substrate specificity of Aeromonas caviae R-enantiomer-specific enoyl-coenzyme A hydratase through site-directed mutagenesis.Characterization and functional analyses of R-specific enoyl coenzyme A hydratases in polyhydroxyalkanoate-producing Ralstonia eutropha.Bacterial itaconate degradation promotes pathogenicity.The crystal structure of PfFabZ, the unique beta-hydroxyacyl-ACP dehydratase involved in fatty acid biosynthesis of Plasmodium falciparum.Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).Cocrystallization and preliminary crystallographic analysis of an inactive MaoC-like hydratase mutant with the substrate crotonyl-CoA.Crystallization and initial X-ray analysis of polyhydroxyalkanoate granule-associated protein from Aeromonas hydrophila Studies on the mechanism of ring hydrolysis in phenylacetate degradation: a metabolic branching point.Production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from plant oil by engineered Ralstonia eutropha strains.Rv0216, a conserved hypothetical protein from Mycobacterium tuberculosis that is essential for bacterial survival during infection, has a double hotdog fold.A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2.A structural model of the plant acyl-acyl carrier protein thioesterase FatB comprises two helix/4-stranded sheet domains, the N-terminal domain containing residues that affect specificity and the C-terminal domain containing catalytic residues.HadD, a novel fatty acid synthase type II protein, is essential for alpha- and epoxy-mycolic acid biosynthesis and mycobacterial fitness.An unusual dehydratase acting on glycerate and a ketoreducatse stereoselectively reducing α-ketone in polyketide starter unit biosynthesis.

P2860

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P2860

Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis

http://www.wikidata.org/entity/Q27639897

description

2003 nî lūn-bûn

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2003 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2003 թվականի հունվարին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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Journal of Biological Chemistry

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Crystal structure of the (R)-s ...... yhydroxyalkanoate biosynthesis

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P2093

Kunio Miki

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

Tadahisa Iwata

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

Takeharu Tsuge

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

Tamao Hisano

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

Toshiaki Fukui

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

Yoshiharu Doi

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P2860

Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency

Recombinant 2-enoyl-CoA hydratase derived from rat peroxisomal multifunctional enzyme 2: role of the hydratase reaction in bile acid synthesis

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

PROCHECK: a program to check the stereochemical quality of protein structures

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme

Structural mechanism of enoyl-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion

Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site

The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule

The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3

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617-24

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scholarly article

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2439185

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10.1074/JBC.M205484200

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1

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278

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2003-01-03T00:00:00Z

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12409309

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crystal structure