Mutagenesis Studies of Human Cystathionine β-Synthase: Residues Important for Heme Binding and Substrate Interactions

Shin-ichi      Ozaki; Chihori      Sakaguchi; Akira      Nakahara; Masahiro      Yoshiya

doi:10.2174/092986610790780233

Abstract

Human cystathionine β-synthase (CBS) is a pyridoxal 5-phosphate (PLP) dependent hemoprotein, which catalyzes the condensation of serine and homocysteine. Our mutagenesis studies suggest that Arg-266 is important to sense structural changes in heme-binding site, and that Gln-222 as well as Tyr-223 are involved in interactions with substrates.

Keywords: Cystathionine, hydrogen sulfide, heme, pyridoxal 5'-phosphate

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Protein & Peptide Letters

Title: Mutagenesis Studies of Human Cystathionine β-Synthase: Residues Important for Heme Binding and Substrate Interactions

Volume: 17 Issue: 3

Author(s): Shin-ichi Ozaki, Chihori Sakaguchi, Akira Nakahara and Masahiro Yoshiya

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Keywords: Cystathionine, hydrogen sulfide, heme, pyridoxal 5'-phosphate

Abstract: Human cystathionine β-synthase (CBS) is a pyridoxal 5-phosphate (PLP) dependent hemoprotein, which catalyzes the condensation of serine and homocysteine. Our mutagenesis studies suggest that Arg-266 is important to sense structural changes in heme-binding site, and that Gln-222 as well as Tyr-223 are involved in interactions with substrates.

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Ozaki Shin-ichi, Sakaguchi Chihori, Nakahara Akira and Yoshiya Masahiro, Mutagenesis Studies of Human Cystathionine β-Synthase: Residues Important for Heme Binding and Substrate Interactions, Protein & Peptide Letters 2010; 17 (3) . https://dx.doi.org/10.2174/092986610790780233