Modulation of Cystathionine β-Synthase Activity by the Arg-51 and Arg-224 Mutations

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概要

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• Human cystathionine β-synthase (CBS) catalyzes a pyridoxal 5′-phosphate (PLP) dependent β-replacement reaction to synthesize cystathionine from serine and homocysteine. The enzyme is unique in bearing not only a catalytically important PLP but also heme. In order to study a regulatory process mediated by heme, we performed mutagenesis of Arg-51 and Arg-224, which have hydrogen-bonding interactions with propionate side chains of the prosthetic group. It was found that the arginine mutations decrease CBS activity by approximately 50%. The results indicate that structural changes in the heme vicinity are transmitted to PLP existing 20 Å away from heme. A possible explanation of our results is discussed on the basis of CBS structure.

• 社団法人 日本農芸化学会の論文
• 2008-09-23

著者

• Ozaki Shin-ichi

  Department Of Biological Sciences Yamaguchi University

• INADA Atsushi

  Department of Biological Sciences, Yamaguchi University

• SADA Kazuya

  Department of Biological Sciences, Yamaguchi University

• Inada Atsushi

  Department Of Biological Sciences Yamaguchi University

• Sada Kazuya

  Department Of Biological Sciences Yamaguchi University

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