Structural basis for substrate specificity of l‐methionine decarboxylase

l ‐Methionine decarboxylase (MetDC) from Streptomyces sp. 590 is a vitamin B6‐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 severa...

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Veröffentlicht in:	Protein science 2021-03, Vol.30 (3), p.663-677
Hauptverfasser:	Okawa, Atsushi, Shiba, Tomoo, Hayashi, Masaya, Onoue, Yuki, Murota, Masaki, Sato, Dan, Inagaki, Junko, Tamura, Takashi, Harada, Shigeharu, Inagaki, Kenji
Format:	Artikel
Sprache:	eng
Schlagworte:	amino acid amino acid decarboxylase Amino acids Amino Acids - chemistry Amino Acids - genetics Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biochemistry & Molecular Biology Carbon dioxide Carboxy-Lyases - chemistry Carboxy-Lyases - genetics Carboxy-Lyases - metabolism Catalysts Catalytic Domain - genetics Crystal structure Decarboxylation Free form Full‐Length Papers Intermediates l ‐methionine decarboxylase Life Sciences & Biomedicine Methionine Methionine decarboxylase Models, Molecular Mutagenesis, Site-Directed Protonation pyridoxal 5′‐phosphate Reaction intermediates reaction mechanism Residues Science & Technology site‐directed mutagenesis Streptomyces Streptomyces - enzymology Streptomyces - genetics Substrate specificity Substrate Specificity - genetics Substrates Vitamin B6 vitamin B6 ‐ dependent enzyme
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