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Biochemical and structural characterization of 5 '-methylthioadenosine nucleosidases from Arabidopsis thaliana
- Authors
- Park, Eun Young; Choi, Woo Suk; Oh, Seung-Ick; Kim, Kyung-Nam; Shin, Jeong Sheop; Song, Hyun Kyu
- Issue Date
- 17-Apr-2009
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Adenine; Crystal structure; Flexible loop; MTA; Nucleosidase; Plant; SAH; Spectroscopic assay
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.381, no.4, pp.619 - 624
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 381
- Number
- 4
- Start Page
- 619
- End Page
- 624
- ISSN
- 0006-291X
- Abstract
- 5'-Methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) are important metabolites in all living organisms. Two similar nucleosidases for hydrolyzing MTA in Arabidopsis thaliana (AtMTAN1 and AtMTAN2) exist, but only AtMTAN2 shows markedly broad substrate specificity for hydrolysis of SAH. To examine the biochemical characteristics of AtMTAN2, it was over-expressed in Escherichia coli and purified to homogeneity. Spectroscopic assays confirm AtMTAN2 catalyzes MTA as well as SAH hydrolysis, compared to AtMTAN1 which only hydrolyzes MTA. In addition, crystal structure of the AtMTAN2 enzyme in complex with, adenine was determined at 2.9 angstrom resolution. Finally, a structural comparison of AtMTAN2 performed with previously determined structures of AtMTAN1 and an E. coli homolog provides clues for the substrate specificity of MTA nucleosidases in A. thaliana. (C) 2009 Elsevier Inc. All rights reserved.
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Related Researcher
- SHIN, Jeong Sheop
- College of Life Sciences and Biotechnology (Division of Life Sciences)