ThYme

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ThYme

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

metasource: bio.tools
version: extracted_at: 2022-11-04T11:34:43.046000

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thyme

metasource: bio.tools
version: extracted_at: 2022-11-04T11:34:43.046000

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Other names: thyme

Thioester-active enzymes

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Publications

More detailed information about this field from each metasource. ×

ThYme: a database for thioester-active enzymes
PMID: 21045059

metasource: bio.tools
version: extracted_at: 2022-11-04T11:34:43.046000

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http://nar.oxfordjournals.org/content/39/suppl_1/D342

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

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• ThYme: a database for thioester-active enzymes PubMed citations: 22.

  22 articles citing: ThYme: a database for thioester-active enzymes

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  Thioesterase enzyme families: Functions, structures, and mechanisms. PMID:34921469

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  Genome-wide identification and analysis of soybean acyl-ACP thioesterase gene family reveals the role of GmFAT to improve fatty acid composition in soybean seed. PMID:34319424

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  Kinetic, Structural, and Mutational Analysis of Acyl-CoA Carboxylase From Thermobifida fusca YX. PMID:33511159

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  Metabolic engineering of β-oxidation to leverage thioesterases for production of 2-heptanone, 2-nonanone and 2-undecanone. PMID:32479802

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  3-Ketoacyl-ACP synthase (KAS) III homologues and their roles in natural product biosynthesis. PMID:31673313

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  RedoxiBase: A database for ROS homeostasis regulated proteins. PMID:31228650

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  Conversion of an amide to a high-energy thioester by Staphylococcus aureus sortase A is powered by variable binding affinity for calcium. PMID:30401805

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  Highly Active C8-Acyl-ACP Thioesterase Variant Isolated by a Synthetic Selection Strategy. PMID:30064208

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  Structural analysis of the dual-function thioesterase SAV606 unravels the mechanism of Michael addition of glycine to an α,β-unsaturated thioester. PMID:28522606

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  Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures. PMID:27530203

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  Microbial production of fatty alcohols. PMID:27465852

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  Structural and Functional Characterization of the PaaI Thioesterase from Streptococcus pneumoniae Reveals a Dual Specificity for Phenylacetyl-CoA and Medium-chain Fatty Acyl-CoAs and a Novel CoA-induced Fit Mechanism. PMID:26538563

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  Discovery of new protein families and functions: new challenges in functional metagenomics for biotechnologies and microbial ecology. PMID:26097471

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  Evolution of acyl-ACP-thioesterases and β-ketoacyl-ACP-synthases revealed by protein-protein interactions. PMID:25110394

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  Structural basis for regulation of the human acetyl-CoA thioesterase 12 and interactions with the steroidogenic acute regulatory protein-related lipid transfer (START) domain. PMID:25002576

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  Functional convergence of structurally distinct thioesterases from cyanobacteria and plants involved in phylloquinone biosynthesis. PMID:24100308

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  ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions. PMID:23193256

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  PeroxiBase: a database for large-scale evolutionary analysis of peroxidases. PMID:23180785

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  Acyl carrier protein structural classification and normal mode analysis. PMID:22374859

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  Prediction of ketoacyl synthase family using reduced amino acid alphabets. PMID:22042516

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  Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity. PMID:21831316

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  Structural classification and properties of ketoacyl synthases. PMID:21830247
• http://nar.oxfordjournals.org/content/39/suppl_1/D342

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More detailed information about this field from each metasource. ×

protein sequence databases

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

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databases of individual protein families

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

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enzymes

metasource: bio.tools
version: extracted_at: 2022-11-04T11:34:43.046000

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small molecules

metasource: bio.tools
version: extracted_at: 2022-11-04T11:34:43.046000

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protein binding sites

metasource: bio.tools
version: extracted_at: 2022-11-04T11:34:43.046000

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gene and protein families

metasource: bio.tools
version: extracted_at: 2022-11-04T11:34:43.046000

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protein folds and structural domains

metasource: bio.tools
version: extracted_at: 2022-11-04T11:34:43.046000

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protein sequence protein family enzyme small molecule protein binding sites gene and protein families protein folds and structural domains