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

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

Affiliation:Department of Biological Sciences, Yamaguchi University, 1677-1 Yoshida, Yamaguchi 753-8515, Japan.

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.

Cite this article as:

Shin-ichi Ozaki, Chihori Sakaguchi, Akira Nakahara and Masahiro Yoshiya, “ Mutagenesis Studies of Human Cystathionine β-Synthase: Residues Important for Heme Binding and Substrate Interactions”, Protein & Peptide Letters (2010) 17: 351. https://doi.org/10.2174/092986610790780233

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