title: Mutagenesis studies of human cystathionine beta-synthase: residues important for heme binding and substrate interactions.
abstract: Human cystathionine beta-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.
authors: Department of Biological Sciences, Yamaguchi University, 1677-1 Yoshida, Yamaguchi, 753-8515, Japan. ozakis@yamaguchi-u.ac.jp
authors: Shin-ichi
authors: S
authors: Ozaki
authors: Chihori
authors: C
authors: Sakaguchi
authors: Akira
authors: A
authors: Nakahara
authors: Masahiro
authors: M
authors: Yoshiya
mesh_terms: D020134:Catalytic Domain; D003541:Cystathionine beta-Synthase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006418:Heme / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006710:Homocysteine / Q000378:metabolism; D006801:Humans; D006862:Hydrogen Sulfide / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed / Q000379:methods*; D011485:Protein Binding; D012694:Serine / Q000378:metabolism; D013053:Spectrophotometry; D013329:Structure-Activity Relationship
chemical_list: D006710:Homocysteine; D006418:Heme; D012694:Serine; D003541:Cystathionine beta-Synthase; D006862:Hydrogen Sulfide