Structural basis for substrate specificity of l ‐methionine decarboxylase
| Autor: | Masaki Murota, Kenji Inagaki, Shigeharu Harada, Yuki Onoue, Dan Sato, Tomoo Shiba, Atsushi Okawa, Masaya Hayashi, Junko Inagaki, Takashi Tamura |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Carboxy-Lyases Stereochemistry Decarboxylation Full‐Length Papers Biochemistry Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Catalytic Domain Amino Acids Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Aromatic L-amino acid decarboxylase Methionine biology Methionine decarboxylase 030302 biochemistry & molecular biology Active site Substrate (chemistry) Streptomyces Amino acid Enzyme chemistry Mutagenesis Site-Directed biology.protein |
| Zdroj: | Protein Sci |
| ISSN: | 1469-896X 0961-8368 |
| Popis: | l ‐Methionine decarboxylase (MetDC) from Streptomyces sp. 590 is a vitamin B(6)‐dependent enzyme and catalyzes the non‐oxidative decarboxylation of l ‐methionine to produce 3‐methylthiopropylamine and carbon dioxide. We present here the crystal structures of the ligand‐free form of MetDC and of several enzymatic reaction intermediates. Group II amino acid decarboxylases have many residues in common around the active site but the residues surrounding the side chain of the substrate differ. Based on information obtained from the crystal structure, and mutational and biochemical experiments, we propose a key role for Gln64 in determining the substrate specificity of MetDC, and for Tyr421 as the acid catalyst that participates in protonation after the decarboxylation reaction. |
| Databáze: | OpenAIRE |
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