Structural insights into the reaction mechanism of S-adenosyl-L-homocysteine hydrolase-Reference-Cited by-同舟云学术

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Structural insights into the reaction mechanism of S-adenosyl-L-homocysteine hydrolase

Published:2015-11-17 Issue:1 Volume:5 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Kusakabe Yoshio,Ishihara Masaaki,Umeda Tomonobu,Kuroda Daisuke,Nakanishi Masayuki,Kitade Yukio,Gouda Hiroaki,Nakamura Kazuo T.,Tanaka Nobutada

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep16641.pdf

Reference52 articles.

1. Cantoni, G. L. Biological methylation: selected aspects. Annu. Rev. Biochem. 44, 435–451 (1975).

2. Tehliverts, O., Malanovic, N., Visram, M., Pavkov-Keller, T. & Keller, W. S-adenosyl-L-homocysteine hydrolase and methylation disorders: Yeast as a model system. Biochim. Biophys. Acta 1832, 204–215 (2013).

3. Dayal, S. et al. Endothelial dysfunction and elevation of S-adenosylhomocysteine in cystathionine β-synthase deficient mice. Circ. Res. 88, 1203–1209 (2001).

4. Baric, I. Inherited disorders in the conversion of methionine to homocysteine. J. Inherit. Metab. Dis. 32, 459–471 (2009).

5. Teng, Y. W., Mehedint, M. G., Garrow, T. A. & Zeisel, S. H. Deletion of betaine-homocysteine S-methyltransferase in mice perturbs choline and 1-carbon metabolism, resulting in fatty liver and hepatocellular carcinomas. J. Biol. Chem. 286, 36258–36267 (2011).

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