首页> Biochemistry> EXAMINING THE STRUCTURAL AND CHEMICAL FLEXIBILITY OF THE ACTIVE SITE BASE, LYS-258, OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE BY REPLACEMENT WITH UNNATURAL AMINO ACIDS

EXAMINING THE STRUCTURAL AND CHEMICAL FLEXIBILITY OF THE ACTIVE SITE BASE, LYS-258, OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE BY REPLACEMENT WITH UNNATURAL AMINO ACIDS

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作者： Gloss LM ^[1] ; Kirsch JF

作者单位： Kirsch JF, UNIV CALIF BERKELEY, DEPT MOLEC & CELL BIOL, DIV BIOCHEM & MOLEC BIOL, BERKELEY, CA 94720, USA ^[1]

关键词 Pyridoxal-5'-phosphate-binding lysine residue Substrate-specificity Directed mutagenesis Bronsted analysis Mutant Catalysis Proteins Cysteine Restoration Mechanism

发布时间 2013-11-20

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Biochemistry

1995年34卷38期

12323-12332页

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EXAMINING THE STRUCTURAL AND CHEMICAL FLEXIBILITY OF THE ACTIVE SITE BASE, LYS-258, OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE BY REPLACEMENT WITH UNNATURAL AMINO ACIDS

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EXAMINING THE STRUCTURAL AND CHEMICAL FLEXIBILITY OF THE ACTIVE SITE BASE, LYS-258, OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE BY REPLACEMENT WITH UNNATURAL AMINO ACIDS

Biochemistry

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