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1. Full Text Crystal structure of human stearoyl-coenzyme A desaturase in complex with substrate
by Wang, Hui and Klein, Michael G and Zou, Hua and Lane, Weston and Snell, Gyorgy and Levin, Irena and Li, Ke and Sang, Bi-Ching and Argonne National Lab. (ANL), Argonne, IL (United States)
Nature Structural and Molecular Biology, ISSN 1545-9993, 07/2015, Volume 22, Issue 7, pp. 581 - 585
Stearoyl-coenzyme A desaturase-1 (SCD1) has an important role in lipid metabolism, and SCD1 inhibitors are potential therapeutic agents for the treatment of... 
BIOCHEMISTRY & MOLECULAR BIOLOGY | OBESE HUMANS | IDENTIFICATION | CARRIER PROTEIN DESATURASE | CELL BIOLOGY | NITRIC-OXIDE REDUCTASE | ENZYME | BIOPHYSICS | GENERATION | MACROMOLECULAR CRYSTALLOGRAPHY | DIIRON PROTEINS | INHIBITORS | COA DESATURASE | Metals - metabolism | Stearoyl-CoA Desaturase - chemistry | Humans | Models, Molecular | Stearoyl-CoA Desaturase - metabolism | Crystallography, X-Ray | Protein Conformation | Acyl Coenzyme A - metabolism | Binding Sites | Acyl Coenzyme A - chemistry | Molecular biology | Enzymes | Crystal structure | Index Medicus
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2. Full Text Lysine Glutarylation Is a Protein Posttranslational Modification Regulated by SIRT5
by Tan, Minjia and Peng, Chao and Anderson, Kristin A and Chhoy, Peter and Xie, Zhongyu and Dai, Lunzhi and Park, Jeongsoon and Chen, Yue and Huang, He and Zhang, Yi and Ro, Jennifer and Wagner, Gregory R and Green, Michelle F and Madsen, Andreas S and Schmiesing, Jessica and Peterson, Brett S and Xu, Guofeng and Ilkayeva, Olga R and Muehlbauer, Michael J and Braulke, Thomas and Mühlhausen, Chris and Backos, Donald S and Olsen, Christian A and McGuire, Peter J and Pletcher, Scott D and Lombard, David B and Hirschey, Matthew D and Zhao, Yingming
Cell Metabolism, ISSN 1550-4131, 04/2014, Volume 19, Issue 4, pp. 605 - 617
We report the identification and characterization of a five-carbon protein posttranslational modification (PTM) called lysine glutarylation (K ). This protein... 
DOMAIN | SUCCINYLATION | METABOLISM | MOUSE MODEL | ENDOCRINOLOGY & METABOLISM | ACETYL-COENZYME-A | CARBAMOYL-PHOSPHATE SYNTHETASE | IDENTIFICATION | NUTRIENT | INSIGHTS | CELL BIOLOGY | Immunoblotting | Protein Processing, Post-Translational - physiology | Acyl Coenzyme A - chemistry | Animals | Carbamoyl-Phosphate Synthase (Ammonia) - metabolism | Models, Biological | Mass Spectrometry | Proteomics | Lysine - metabolism | Mice | Molecular Structure | Lysine - chemistry | Acyl Coenzyme A - metabolism | Sirtuins - metabolism | Post-translational modification | Phosphates | Urea | Enzymes | Lysine | Analysis | Physiological aspects | Mass spectrometry | Index Medicus
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3. Full Text A novel role for coenzyme a during hydride transfer in 3-hydroxy-3- methylglutaryl-coenzyme a reductase
by Steussy, C. Nicklaus and Critchelow, Chandra J and Schmidt, Tim and Min, Jung-Ki and Wrensford, Louise V and Burgner, John W and Rodwell, Victor W and Stauffacher, Cynthia V and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Biochemistry, ISSN 0006-2960, 08/2013, Volume 52, Issue 31, pp. 5195 - 5205
In this study, we take advantage of the ability of HMG-CoA reductase (HMGR) from Pseudomonas mevalonii to remain active while in its crystallized form to study... 
MACROMOLECULAR REFINEMENT | SYSTEM | CATALYSIS | PROTEIN | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | HMG-COA REDUCTASE | CRYSTAL-STRUCTURES | CRYSTALLOGRAPHY | PSEUDOMONAS-MEVALONII | IDENTIFICATION | Catalytic Domain | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Coenzyme A - chemistry | Models, Molecular | Acyl Coenzyme A - genetics | Coenzyme A - metabolism | Acyl Coenzyme A - chemistry | Pseudomonas - enzymology | Bacterial Proteins - metabolism | Catalysis | Kinetics | Acyl Coenzyme A - metabolism | Pseudomonas - chemistry | Pseudomonas - genetics | Index Medicus
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4. Full Text A synthetic pathway for the fixation of carbon dioxide in vitro
by Schwander, Thomas and Von Borzyskowski, Lennart Schada and Burgener, Simon and Cortina, Niña Socorro and Erb, Tobias J
Science, ISSN 0036-8075, 11/2016, Volume 354, Issue 6314, pp. 900 - 904
Carbon dioxide (CO2) is an important carbon feedstock for a future green economy. This requires the development of efficient strategies for its conversion into... 
ENERGY | ENZYME | EVOLUTION | CROTONYL-COA CARBOXYLASE/REDUCTASE | MULTIDISCIPLINARY SCIENCES | BIOLOGY | PLANTS | RUBISCO | PHOTORESPIRATORY BYPASS | FUTURE | PHOTOSYNTHESIS | Rhodobacter sphaeroides - enzymology | Carbon Dioxide - chemistry | Synthetic Biology | Arabidopsis - enzymology | Carbon Cycle | Oxidoreductases - genetics | Protein Engineering | Acyl Coenzyme A - genetics | Biosynthetic Pathways | Oxidoreductases - chemistry | Carbon - chemistry | Acyl Coenzyme A - chemistry | Enzymes | Carbon dioxide | Chemical properties | Research | Carbon fixation | Chemical research | Molecules | Chemical synthesis | Index Medicus | Fixation | Pathways | Organisms | In vitro testing | Biomass | Carbon
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5. Full Text The AibR-isovaleryl coenzyme A regulator and its DNA binding site – a model for the regulation of alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus
by Bock, Tobias and Volz, Carsten and Hering, Vanessa and Scrima, Andrea and Müller, Rolf and Blankenfeldt, Wulf
Nucleic Acids Research, ISSN 0305-1048, 2017, Volume 45, Issue 4, pp. 2166 - 2178
Isovaleryl coenzyme A (IV-CoA) is an important building block of iso-fatty acids. In myxobacteria, IV-CoA is essential for the formation of signaling molecules... 
COMPLEX | FATTY-ACID BIOSYNTHESIS | OPERATOR | STRUCTURAL BASIS | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | TETR FAMILY | REPRESSOR | IDENTIFICATION | TRANSCRIPTIONAL REGULATION | COA SYNTHASE | Promoter Regions, Genetic | Transcription Factors - chemistry | Operon | Molecular Conformation | Bacterial Proteins - genetics | Myxococcus xanthus - genetics | Models, Molecular | Acyl Coenzyme A - genetics | Myxococcus xanthus - metabolism | Acyl Coenzyme A - chemistry | Transcription Factors - metabolism | Base Sequence | Bacterial Proteins - metabolism | Gene Expression Regulation, Bacterial | Acyl Coenzyme A - metabolism | Binding Sites | Index Medicus | Structural Biology
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6. Full Text One-Step Transformation of Coenzyme A into Analogues by Transamidation
by Sanichar, Randy and Vederas, John C
Organic Letters, ISSN 1523-7060, 04/2017, Volume 19, Issue 8, pp. 1950 - 1953
Several coenzyme A (CoA) analogues are made in a single step under mild conditions via transamidation reactions catalyzed by boric acid in water. This approach... 
ACTIVATION | COA | AMINES | NONRIBOSOMAL PEPTIDE SYNTHETASES | CHEMOENZYMATIC SYNTHESIS | ENZYMES | CHEMISTRY, ORGANIC | CARBOXAMIDES | PANTETHEINE | CATALYST | PROTEINS | Water | Acyl Carrier Protein - chemistry | Polyketide Synthases - chemistry | Temperature | Boric Acids - chemistry | Peptide Synthases - chemistry | Cysteamine - chemistry | Coenzyme A - chemistry | Molecular Structure | Time | Catalysis | Fatty Acid Synthases - chemistry | Index Medicus
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7. Full Text DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different Acyl-CoA specificities
by Jennings, Benjamin C and Linder, Maurine E
Journal of Biological Chemistry, ISSN 0021-9258, 03/2012, Volume 287, Issue 10, pp. 7236 - 7245
DHHCproteins catalyze the reversible S-acylation of proteins at cysteine residues, a modification important for regulating protein localization, stability, and... 
LOCALIZATION | ACYLATION | MEDIATED PALMITOYLATION | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRAFFICKING | HIP14 | IDENTIFICATION | HUNTINGTIN | ARACHIDONATE | Lipoylation - physiology | Tumor Suppressor Proteins - metabolism | Palmitoyl Coenzyme A - chemistry | Palmitoyl Coenzyme A - metabolism | Substrate Specificity - physiology | Acyl Coenzyme A - genetics | Acyltransferases - metabolism | Acyltransferases - genetics | Palmitoyl Coenzyme A - genetics | Acyl Coenzyme A - chemistry | Acylation - physiology | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Acyltransferases - chemistry | Kinetics | Acyl Coenzyme A - metabolism | Index Medicus | Fatty Acylation | Membrane Enzymes | Fatty Acid | G Proteins | Post-translational Modification | Lck | Palmitoylation | S-Acylation | Enzymology | Acyltransferase
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8. Full Text Thermophilic Coenzyme B12-Dependent Acyl Coenzyme A (CoA) Mutase from Kyrpidia tusciae DSM 2912 Preferentially Catalyzes Isomerization of (R)-3-Hydroxybutyryl-CoA and 2-Hydroxyisobutyryl-CoA
by Weichler, Maria-Teresa and Kurteva-Yaneva, Nadya and Przybylski, Denise and Schuster, Judith and Müller, Roland H and Harms, Hauke and Rohwerder, Thore
Applied and environmental microbiology, ISSN 0099-2240, 07/2015, Volume 81, Issue 14, pp. 4564 - 4572
The recent discovery of a coenzyme B12-dependent acyl-coenzyme A (acyl-CoA) mutase isomerizing 3-hydroxybutyryl- and 2-hydroxyisobutyryl-CoA in the mesophilic... 
Cobamides - metabolism | Intramolecular Transferases - genetics | Stereoisomerism | Bacillales - chemistry | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Enzyme Stability | Substrate Specificity | Acyl Coenzyme A - chemistry | Intramolecular Transferases - metabolism | Bacillales - enzymology | Bacillales - genetics | Bacillales - metabolism | Bacterial Proteins - metabolism | Catalysis | Intramolecular Transferases - chemistry | Acyl Coenzyme A - metabolism | Index Medicus | Biotechnology
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9. Full Text The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A
by Gulick, Andrew M and Starai, Vincent J and Horswill, Alexander R and Homick, Kristen M and Escalante-Semerena, Jorge C
Biochemistry, ISSN 0006-2960, 03/2003, Volume 42, Issue 10, pp. 2866 - 2873
Acetyl-coenzyme A synthetase catalyzes the two-step synthesis of acetyl-CoA from acetate, ATP, and CoA and belongs to a family of adenylate-forming enzymes... 
FORMING ENZYME SUPERFAMILY | SALMONELLA-ENTERICA | LIKELIHOOD DENSITY MODIFICATION | FIREFLY LUCIFERASE | NONRIBOSOMAL PEPTIDE SYNTHETASES | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | TYROCIDINE SYNTHETASE-1 | PENICILLIUM-CHRYSOGENUM | ADENYLATION DOMAINS | SITE-DIRECTED MUTAGENESIS | Binding, Competitive | Acetate-CoA Ligase - isolation & purification | Amino Acid Sequence | Acetate-CoA Ligase - chemistry | Adenosine Monophosphate - chemistry | Bacterial Proteins - chemistry | Crystallization | Coenzyme A - chemistry | Coenzyme A Ligases - antagonists & inhibitors | Molecular Sequence Data | Crystallography, X-Ray | Acyl Coenzyme A - chemistry | Coenzyme A Ligases - chemistry | Enzyme Inhibitors - chemistry | Salmonella enterica - enzymology | Protein Conformation | Acetylation | Bacterial Proteins - isolation & purification | Binding Sites | Index Medicus
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10. Full Text Expression and characterization of a PNPLA3 protein isoform (I148M) associated with nonalcoholic fatty liver disease
by Huang, Yongcheng and Cohen, Jonathan C and Hobbs, Helen H
Journal of Biological Chemistry, ISSN 0021-9258, 10/2011, Volume 286, Issue 43, pp. 37085 - 37093
A genetic variant of PNPLA3 (patatin-like phospholipase domain-containing 3; PNPLA3-I148M), a serine protease of unknown function, is associated with... 
ADIPOSE TRIGLYCERIDE LIPASE | GENE | CGI-58 | BIOCHEMISTRY & MOLECULAR BIOLOGY | PATATIN | SUSCEPTIBILITY | ESTERS | CHANARIN-DORFMAN-SYNDROME | FAMILY | Humans | Substrate Specificity | Acyl Coenzyme A - genetics | Isoenzymes - chemistry | Mutation, Missense | Triglycerides - chemistry | Isoenzymes - metabolism | Fatty Liver - enzymology | Non-alcoholic Fatty Liver Disease | Membrane Proteins - metabolism | Phospholipids - metabolism | Acyl Coenzyme A - metabolism | Fatty Liver - genetics | Recombinant Proteins - metabolism | Cell Line | Isoenzymes - genetics | Membrane Proteins - genetics | Phospholipids - chemistry | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Lipase - metabolism | Lipase - chemistry | Phospholipids - genetics | Acyl Coenzyme A - chemistry | Triglycerides - metabolism | Hydrolysis | Membrane Proteins - chemistry | Triglycerides - genetics | Amino Acid Substitution | Lipase - genetics | Index Medicus | Glycerolipid | Fatty Acid Metabolism | PNPLA3 | Lipids | Hydrolases | Lipid Metabolism | Adiponutrin | Triglyceride
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11. Full Text Pathways for Arene Oxidation in Non-Heme Diiron Enzymes: Lessons from Computational Studies on Benzoyl Coenzyme A Epoxidase
by Rokob, Tibor András
Journal of the American Chemical Society, ISSN 0002-7863, 11/2016, Volume 138, Issue 44, pp. 14623 - 14638
Oxygenation of aromatic rings using O-2 is catalyzed by several non-heme carboxylate-bridged diiron enzymes. In order to provide a general mechanistic... 
DIOXYGEN ACTIVATION | METHANE MONOOXYGENASE | BENZENE HYDROXYLATION | INTRAMOLECULAR AROMATIC HYDROXYLATION | TOLUENE/O-XYLENE MONOOXYGENASE | BACTERIAL MULTICOMPONENT MONOOXYGENASES | CIS-DIHYDROXYLATION | PHENOL HYDROXYLASE | FUNCTIONAL-MODEL | CHEMISTRY, MULTIDISCIPLINARY | C-H | Alkenes - chemistry | Oxidation-Reduction | Computer Simulation | Epoxy Compounds - chemistry | Iron - chemistry | Oxygen - chemistry | Models, Molecular | Coordination Complexes | Nonheme Iron Proteins - chemistry | Oxidoreductases - chemistry | Acyl Coenzyme A - chemistry | Computational chemistry | Chemistry, Organic | Research | Chemical properties | Electric properties | Index Medicus
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12. Full Text OleA Glu117 is key to condensation of two fatty-acyl coenzyme A substrates in long-chain olefin biosynthesis
by Jensen, Matthew R and Goblirsch, Brandon R and Christenson, James K and Esler, Morgan A and Mohamed, Fatuma A and Wackett, Lawrence P and Wilmot, Carrie M and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Biochemical Journal, ISSN 0264-6021, 12/2017, Volume 474, Issue 23, pp. 3871 - 3886
In the interest of decreasing dependence on fossil fuels, microbial hydrocarbon biosynthesis pathways are being studied for renewable, tailored production of... 
THIOLASE | COMPLEX | KETOSYNTHASE | TO-HEAD CONDENSATION | PATHWAY | CRYSTAL-STRUCTURE | BIOCHEMISTRY | BIOCHEMISTRY & MOLECULAR BIOLOGY | INTERMEDIATE | 3-HYDROXY-3-METHYLGLUTARYL-COA SYNTHASE | HYDROCARBON | Glutamic Acid - genetics | Ligases - genetics | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Xanthomonas campestris - genetics | Acyl Coenzyme A - genetics | Crystallography, X-Ray | Ligases - chemistry | Mutation, Missense | Acyl Coenzyme A - chemistry | Alkenes - chemistry | Alkenes - metabolism | Xanthomonas campestris - enzymology | Amino Acid Substitution | Glutamic Acid - chemistry | Index Medicus | BASIC BIOLOGICAL SCIENCES | INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
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13. Full Text The pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is a fatty acid-binding protein
by Darwiche, Rabih and Mène-Saffrané, Laurent and Gfeller, David and Asojo, Oluwatoyin A and Schneiter, Roger
Journal of Biological Chemistry, ISSN 0021-9258, 05/2017, Volume 292, Issue 20, pp. 8304 - 8314
Members of the CAP superfamily (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins), also known as SCP superfamily (sperm-coating... 
DOMAIN | GENE | MECHANISM | VENOM ALLERGEN | BIOCHEMISTRY & MOLECULAR BIOLOGY | EXPORT | INHIBITOR | SACCHAROMYCES-CEREVISIAE | MOTIF | REVEALS | Microfilament Proteins - chemistry | Mutagenesis, Site-Directed | Coenzyme A Ligases - genetics | Saccharomyces cerevisiae - genetics | Acyl Coenzyme A - genetics | Fatty Acid-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Fatty Acid-Binding Proteins - genetics | Saccharomyces cerevisiae - chemistry | Acyl Coenzyme A - chemistry | Coenzyme A Ligases - metabolism | Saccharomyces cerevisiae - metabolism | Coenzyme A Ligases - chemistry | Computer Simulation | Saccharomyces cerevisiae Proteins - metabolism | Protein Domains | Fatty Acid-Binding Proteins - chemistry | Microfilament Proteins - metabolism | Acyl Coenzyme A - metabolism | Microfilament Proteins - genetics | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus | secretion | sterol | fatty acid | fatty acid binding protein | CAP protein family | acyl-CoA synthetase | cholesterol | Metabolism | fatty acid transport | Saccharomyces cerevisiae
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14. Full Text X-ray structure of a mammalian stearoyl-CoA desaturase
by Bai, Yonghong and McCoy, Jason G and Levin, Elena J and Sobrado, Pablo and Rajashankar, Kanagalaghatta R and Fox, Brian G and Zhou, Ming and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature, ISSN 0028-0836, 08/2015, Volume 524, Issue 7564, pp. 252 - 256
Stearoyl-CoA desaturase (SCD) is conserved in all eukaryotes and introduces the first double bond into saturated fatty acyl-CoAs1-4. Because the... 
RIBONUCLEOTIDE REDUCTASE | SUBSTRATE-SPECIFICITY | ENZYME | MECHANISM | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | DIIRON PROTEINS | FATTY-ACID DESATURATION | IDENTIFICATION | COENZYME-A DESATURASE | SACCHAROMYCES-CEREVISIAE | Protein Structure, Tertiary | Electron Transport | Models, Molecular | Crystallography, X-Ray | Structure-Activity Relationship | Histidine - metabolism | Cytochromes b5 - chemistry | Cytochromes b5 - metabolism | Static Electricity | Iron - metabolism | Oxygen - metabolism | Acyl Coenzyme A - chemistry | Animals | Stearoyl-CoA Desaturase - chemistry | Stearoyl-CoA Desaturase - metabolism | Mice | Histidine - chemistry | Acyl Coenzyme A - metabolism | Binding Sites | Physiological aspects | Eukaryotes | Genetic aspects | Phospholipids | Mammals | Analysis | Proteins | Cytochrome | Enzymes | Lipids | Binding sites | Crystal structure | Index Medicus
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15. Full Text An acyltransferase domain of FK506 polyketide synthase recognizing both an acyl carrier protein and coenzyme A as acyl donors to transfer allylmalonyl and ethylmalonyl units
by Jiang, Hui and Wang, Yue‐Yue and Guo, Yuan‐Yang and Shen, Jie‐Jie and Zhang, Xiao‐Sheng and Luo, Hong‐Dou and Ren, Ni‐Ni and Jiang, Xin‐Hang and Li, Yong‐Quan
FEBS Journal, ISSN 1742-464X, 07/2015, Volume 282, Issue 13, pp. 2527 - 2539
An acyltransferase ( AT ) of FK 506 biosynthetic polyketide synthase ( PKS ), AT 4 FkbB recognizes an acyl carrier protein ( ACP ), ACP T csA as an acyl donor... 
acyl donor | acyl carrier protein | acyl unit | polyketide | acyltransferase | Polyketide | Acyl unit | Acyltransferase | Acyl carrier protein | Acyl donor | Protein Structure, Tertiary | Streptomyces - metabolism | Acyl Carrier Protein - chemistry | Multigene Family | Polyketide Synthases - chemistry | Base Sequence | Coenzyme A - chemistry | Molecular Sequence Data | Substrate Specificity | Acyltransferases - chemistry | Tacrolimus - metabolism | Chromatography, High Pressure Liquid | Enzymes | Yuan (China) | Thiols | Analysis | Immunosuppressive agents | Proteins | Molecular biology | Index Medicus
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