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animals (67) 67
enoyl-coa hydratase - metabolism (59) 59
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biochemistry & molecular biology (51) 51
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Applied microbiology and biotechnology, ISSN 1432-0614, 2018, Volume 102, Issue 14, pp. 5841 - 5858
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 11/2012, Volume 287, Issue 45, pp. 37986 - 37996
... of this pathway and show another stable complex, PaaFG, an enoyl-CoA hydratase and enoyl-Coa isomerase, both belonging... 
THIOLASE | ANGSTROM RESOLUTION | AEROBIC METABOLISM | COA HYDRATASE | COENZYME | ACID | MECHANISM | DELTA-DELTA-ENOYL-COA ISOMERASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING | REVEALS | Enoyl-CoA Hydratase - genetics | Models, Chemical | Enoyl-CoA Hydratase - chemistry | Protein Multimerization | Crystallography, X-Ray | Phenylacetates - chemistry | Dodecenoyl-CoA Isomerase | Multiprotein Complexes - metabolism | Escherichia coli - metabolism | Protein Structure, Quaternary | Water - chemistry | Carbon-Carbon Double Bond Isomerases - chemistry | Molecular Structure | Acetyl Coenzyme A - chemistry | Protein Structure, Tertiary | Catalytic Domain | Escherichia coli - enzymology | Oxidation-Reduction | Protein Structure, Secondary | Enoyl-CoA Hydratase - metabolism | Water - metabolism | Models, Molecular | Escherichia coli Proteins - metabolism | Phenylacetates - metabolism | Microscopy, Electron | Operon - genetics | Acetyl Coenzyme A - metabolism | Carbon-Carbon Double Bond Isomerases - metabolism | Multiprotein Complexes - ultrastructure | Multiprotein Complexes - chemistry | Carbon-Carbon Double Bond Isomerases - genetics | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Escherichia coli Proteins - chemistry | Enzyme Structure | Protein Complexes | Protein Crystallization | Enzyme Catalysis | Phenylacetate Degradation | Enzymology | Metabolism | Aromatic Compounds Degradation Pathway | Beta-Oxidation
Journal Article
Journal Article
Journal Article
CHEMCATCHEM, ISSN 1867-3880, 01/2018, Volume 10, Issue 2, pp. 407 - 414
Recently, the enzyme family of oleate hydratases (OHs: EC 4.2.1.53) has gained increasing scientific and economic interest, as these FAD-binding bacterial enzymes do not require cofactor recycling and possess high thermal and pH stability... 
protein structure | 10-HYDROXYSTEARIC ACID | fatty acids | DOUBLE-BOND HYDRATASE | MECHANISM | RECOMBINANT ESCHERICHIA-COLI | oleate hydratase | hydration | OLEIC-ACID | CHEMISTRY, PHYSICAL | lyases
Journal Article
Angewandte Chemie (International ed.), ISSN 1433-7851, 2019, Volume 58, Issue 1, pp. 173 - 177
Journal Article
Journal Article