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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 17, Issue 3, 2010

Page: [351 - 355] Pages: 5

DOI: 10.2174/092986610790780233

Price: $65

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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