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Protein & Peptide Letters

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

DOI: 10.2174/092986610790780233

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

Page: [351 - 355] Pages: 5

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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