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1. Full Text Aspartase/Fumarase Superfamily: A Common Catalytic Strategy Involving General Base-Catalyzed Formation of a Highly Stabilized aci -Carboxylate Intermediate
by Puthan Veetil, Vinod and Fibriansah, Guntur and Raj, Hans and Thunnissen, Andy-Mark W. H and Poelarends, Gerrit J
Biochemistry (Easton), ISSN 0006-2960, 05/2012, Volume 51, Issue 21, pp. 4237 - 4243
CHEMICAL MECHANISM | ACTIVE-SITE | ARGININOSUCCINATE LYASE | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | 3-CARBOXY-CIS,CIS-MUCONATE LACTONIZING ENZYME | BACILLUS SP YM55-1 | ASPARTATE AMMONIA-LYASE | SUBTILIS ADENYLOSUCCINATE LYASE | SITE-DIRECTED MUTAGENESIS | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Argininosuccinate Lyase - chemistry | Intramolecular Lyases - metabolism | Saccharomyces cerevisiae - genetics | Humans | Aspartate Ammonia-Lyase - chemistry | Fumarate Hydratase - chemistry | delta-Crystallins - metabolism | Molecular Sequence Data | Substrate Specificity | delta-Crystallins - genetics | Aspartate Ammonia-Lyase - metabolism | Argininosuccinate Lyase - metabolism | Aspartate Ammonia-Lyase - genetics | Adenylosuccinate Lyase - chemistry | Fumarate Hydratase - metabolism | Protein Structure, Quaternary | Conserved Sequence | Adenylosuccinate Lyase - genetics | Catalysis | Protein Structure, Tertiary | Amino Acid Sequence | Catalytic Domain | Argininosuccinate Lyase - genetics | Escherichia coli - enzymology | Models, Molecular | Escherichia coli Proteins - metabolism | Fumarate Hydratase - genetics | Saccharomyces cerevisiae Proteins - genetics | Sequence Homology, Amino Acid | delta-Crystallins - chemistry | Intramolecular Lyases - genetics | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Escherichia coli Proteins - genetics | Saccharomyces cerevisiae - enzymology | Adenylosuccinate Lyase - metabolism | Escherichia coli Proteins - chemistry | Intramolecular Lyases - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Enzyme binding | Fumarase | Chemical properties | Structure | Analysis | Index Medicus
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2. Full Text Pseudomonas fluorescens Strain R124 Encodes Three Different MIO Enzymes
by Csuka, Pál and Juhász, Vivien and Kohári, Szabolcs and Filip, Alina and Varga, Andrea and Sátorhelyi, Péter and Bencze, László Csaba and Barton, Hazel and Paizs, Csaba and Poppe, László
Chembiochem : a European journal of chemical biology, ISSN 1439-4227, 02/2018, Volume 19, Issue 4, pp. 411 - 418
gene transfer | phenylalanine | nitrogen | biocatalysis | lyases | Pharmacology & Pharmacy | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Chemistry, Medicinal | Science & Technology | Biocatalysis | Ammonia-Lyases - genetics | Histidine Ammonia-Lyase - genetics | Pseudomonas fluorescens - isolation & purification | Ammonia-Lyases - metabolism | Histidine Ammonia-Lyase - metabolism | Pseudomonas fluorescens - genetics | Phenylalanine Ammonia-Lyase - chemistry | Phenylalanine Ammonia-Lyase - metabolism | Phenylalanine Ammonia-Lyase - genetics | Histidine Ammonia-Lyase - chemistry | Pseudomonas fluorescens - enzymology | Molecular Structure | Ammonia-Lyases - chemistry | Enzymes | Ammonia | Histidine | Fixation | Phenylalanine | Physiological aspects | Catalysis | Enantiomers | Nitrogen | Tyrosine | Transformation | Gene transfer | Amino acids | Pseudomonas fluorescens | Metabolism | Biocatalysts | Thermal stability | Substrates | Nitrogen metabolism | Nitrogen fixation | Index Medicus
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3. Full Text Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism, intracellular growth, and virulence
by Muñoz‐Elías, Ernesto J and Upton, Anna M and Cherian, Joseph and McKinney, John D
Molecular microbiology, ISSN 0950-382X, 06/2006, Volume 60, Issue 5, pp. 1109 - 1122
Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Microbiology | Science & Technology | Fundamental and applied biological sciences. Psychology | Biological and medical sciences | Propionates - metabolism | Isocitrate Lyase - classification | Isocitrate Lyase - genetics | Isocitrate Lyase - metabolism | Molecular Sequence Data | Male | Phylogeny | Isoenzymes - classification | Carbon-Carbon Lyases - genetics | Citric Acid - chemistry | Isoenzymes - metabolism | Mycobacterium tuberculosis - physiology | Female | Citrate (si)-Synthase - metabolism | Hydro-Lyases - metabolism | Molecular Structure | Hydro-Lyases - genetics | Bone Marrow Cells - cytology | Isoenzymes - genetics | Mice, Inbred C57BL | Cells, Cultured | Carbon-Carbon Lyases - classification | Escherichia coli Proteins - metabolism | Macrophages - cytology | Macrophages - metabolism | Animals | Citrate (si)-Synthase - genetics | Escherichia coli Proteins - genetics | Carbon-Carbon Lyases - metabolism | Citric Acid - metabolism | Mice | Bone Marrow Cells - metabolism | Mycobacterium tuberculosis - genetics | Physiological aspects | Growth | Tuberculosis | Fungi | Pathogens | Bacteria | Metabolism | Fatty acids | Genes | Index Medicus
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4. Full Text Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle
by Verschueren, Koen H. G and Blanchet, Clement and Felix, Jan and Dansercoer, Ann and De Vos, Dirk and Bloch, Yehudi and Van Beeumen, Jozef and Svergun, Dmitri and Gutsche, Irina and Savvides, Savvas N and Verstraete, Kenneth
Nature (London), ISSN 0028-0836, 04/2019, Volume 568, Issue 7753, pp. 571 - 575
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Biocatalysis | Humans | ATP Citrate (pro-S)-Lyase - genetics | Models, Molecular | Crystallography, X-Ray | ATP Citrate (pro-S)-Lyase - chemistry | Methanosarcinales - enzymology | Citric Acid Cycle | Methanosarcinales - genetics | Chlorobium - genetics | Chlorobium - enzymology | ATP Citrate (pro-S)-Lyase - metabolism | Evolution, Molecular | Origin | Citrate synthase | Analysis | ATP synthesis | Lyases | Structure | Krebs cycle | Metabolites | Resveratrol | Crystals | Physiological aspects | Histones | Evolution | Fatty acids | Citryl-CoA lyase | Tricarboxylic acid cycle | Adipose tissue | Carbon dioxide | Lipids | Proteins | Coenzyme A | Lipid metabolism | Acetylation | Catalysis | Chemical synthesis | Crystal structure | Carbohydrates | Enzymes | Adenosine | Prokaryotes | Hyperlipidemia | Carbohydrate metabolism | Metabolism | Cholesterol | Substrates | Cholinergics | Microscopy | Software | Acetylcholine | ATP | Binding sites | Index Medicus | Life Sciences | Methanosarcinales | Biochemistry, Molecular Biology | Biomolecules | ATP Citrate (pro-S)-Lyase | Chlorobium
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5. Full Text Synthetic and Therapeutic Applications of Ammonia-lyases and Aminomutases
by Parmeggiani, Fabio and Weise, Nicholas J and Ahmed, Syed T and Turner, Nicholas J
Chemical reviews, ISSN 0009-2665, 01/2018, Volume 118, Issue 1, pp. 73 - 118
Physical Sciences | Chemistry | Chemistry, Multidisciplinary | Science & Technology | Phenylalanine Ammonia-Lyase - classification | Biocatalysis | Humans | Models, Molecular | Substrate Specificity | Ammonia-Lyases - metabolism | Transaminases - classification | Phenylalanine Ammonia-Lyase - chemistry | Phenylalanine Ammonia-Lyase - metabolism | Intramolecular Transferases - metabolism | Ammonia-Lyases - therapeutic use | Ammonia-Lyases - classification | Transaminases - metabolism | Bacteria - enzymology | Intramolecular Transferases - therapeutic use | Transaminases - therapeutic use | Intramolecular Transferases - classification | Ammonia | Enzymes | Biotechnology | Pathology | Catalysts | Isomerization | Fine chemicals | Cascades | Amino acids | Index Medicus
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6. Full Text Characterization of a bifunctional alginate lyase as a new member of the polysaccharide lyase family 17 from a marine strain BP-2
by Huang, Guiyuan and Wen, Shunhua and Liao, Siming and Wang, Qiaozhen and Pan, Shihan and Zhang, Rongcan and Lei, Fu and Liao, Wei and Feng, Jie and Huang, Shushi
Biotechnology letters, ISSN 0141-5492, 10/2019, Volume 41, Issue 10, pp. 1187 - 1200
Life Sciences | Biochemistry, general | Biotechnology | Bifunctional alginate lyase | Microbiology | Alginate oligosaccharides | Applied Microbiology | Marine strain | Bioenergy | Polysaccharide lyase family 17 | Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Science & Technology | Polysaccharide-Lyases - metabolism | Temperature | Molecular Weight | Substrate Specificity | Gammaproteobacteria - classification | Alginates - metabolism | Aquatic Organisms - enzymology | Gammaproteobacteria - genetics | Polysaccharide-Lyases - chemistry | Alginic Acid - metabolism | Aquatic Organisms - isolation & purification | Aquatic Organisms - genetics | Gammaproteobacteria - enzymology | Polysaccharide-Lyases - genetics | Polysaccharide-Lyases - isolation & purification | Enzyme Stability | Polysaccharides, Bacterial - metabolism | Enzyme Inhibitors - analysis | Oligosaccharides - metabolism | Aquatic Organisms - classification | Gammaproteobacteria - isolation & purification | Hydrolysis | Sargassum - microbiology | Enzyme Activators - analysis | Monosaccharides - metabolism | Hydrogen-Ion Concentration | Identification and classification | Polysaccharides | Lyases | Enzyme activity | Calcium | Alginic acid | Alginate lyase | pH effects | Molecular weight | Monosaccharides | Enzymatic activity | Low molecular weights | Substrate specificity | Freeze-drying | Metal ions | Carbohydrates | Enzymes | Algae | Ions | Substrate inhibition | Mass spectroscopy | Oligosaccharides | Fermentation | Substrates | Zinc | Chromatography | Ion exchanging | Thin layer chromatography | Acids | Sodium | Thin-layer chromatography | Dialysis | Sodium alginate | Mass spectrometry | Calcium ions | Drying | Index Medicus
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7. Full Text Selectivity of commonly used pharmacological inhibitors for cystathionine β synthase (CBS) and cystathionine γ lyase (CSE)
by Asimakopoulou, Antonia and Panopoulos, Panagiotis and Chasapis, Christos T and Coletta, Ciro and Zhou, Zongmin and Cirino, Giuseppe and Giannis, Athanassios and Szabo, Csaba and Spyroulias, Georgios A and Papapetropoulos, Andreas
British journal of pharmacology, ISSN 0007-1188, 06/2013, Volume 169, Issue 4, pp. 922 - 932
DL‐propargylglycine | nitric oxide | hydrogen sulfide | cystathionine γ‐lyase | pyridoxal‐5′‐phosphate | cystathionine β‐synthase | aminooxyacetic acid | β‐cyano‐L‐alanine | cystathionine γ-lyase | DL-propargylglycine | cystathionine β-synthase | β-cyano-L-alanine | pyridoxal-5′-phosphate | Hydrogen Sulfide - metabolism | Glycine - analogs & derivatives | Cystathionine beta-Synthase - antagonists & inhibitors | Humans | Cystathionine gamma-Lyase - metabolism | Recombinant Fusion Proteins - metabolism | Alanine - analogs & derivatives | Glutathione Transferase - genetics | Alkynes - pharmacology | Aorta, Thoracic - drug effects | Cystathionine gamma-Lyase - genetics | Nitric Oxide Donors - pharmacology | Cystathionine beta-Synthase - genetics | Peptide Fragments - genetics | Alanine - pharmacology | Peptide Fragments - metabolism | Enzyme Inhibitors - pharmacology | Aorta, Thoracic - metabolism | Glutathione Transferase - metabolism | Rats | Cystathionine beta-Synthase - metabolism | Recombinant Fusion Proteins - chemistry | Glutathione Transferase - chemistry | Cystathionine gamma-Lyase - antagonists & inhibitors | Rats, Sprague-Dawley | Hydrogen Sulfide - analysis | Aorta, Thoracic - enzymology | Animals | Glycine - pharmacology | Kinetics | Vasodilation - drug effects | In Vitro Techniques | Nitric Oxide - metabolism | Index Medicus | Research Papers
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