Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine γ-lyase with substrates
| Autor: | E. A. Morozova, R. M. Khomutov, L.N. Zakomirdina, Alexey D. Nikulin, Tatyana V. Demidkina, S.V. Revtovich, E. N. Khurs |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Stereochemistry Biochemistry Substrate Specificity chemistry.chemical_compound Bacterial Proteins Organic chemistry Cysteine Enzyme Inhibitors Pyridoxal chemistry.chemical_classification Methionine Binding Sites biology Active site General Medicine biology.organism_classification Lyase Amino acid Citrobacter freundii Carbon-Sulfur Lyases Kinetics Enzyme chemistry Covalent bond biology.protein Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Biochemistry. Biokhimiia. 76(5) |
| ISSN: | 1608-3040 |
| Popis: | Crystal structures of Citrobacter freundii methionine γ-lyase complexes with the substrates of γ- (L-1-amino-3-methylthiopropylphosphinic acid) and β- (S-ethyl-L-cysteine) elimination reactions and the competitive inhibitor L-norleucine have been determined at 1.45, 1.8, and 1.63 Å resolution, respectively. All three amino acids occupy the active site of the enzyme but do not form a covalent bond with pyridoxal 5'-phosphate. Hydrophobic interactions between the active site residues and the side groups of the substrates and the inhibitor are supposed to cause noncovalent binding. Arg374 and Ser339 are involved in the binding of carboxyl groups of the substrates and the inhibitor. The hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acids. |
| Databáze: | OpenAIRE |
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