ID | 34247 |
FullText URL | |
Author |
Fujitani, Yoshiyuki
Horiuchi, Terumi
Ito, Kazutoshi
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Abstract | Several D-amino acids have been identified in plants. However, the biosynthetic pathway to them is unclear. In this study, we cloned and sequenced a cDNA encoding a serine racemase from barley which contained an open reading frame encoding 337 amino acid residues. The deduced amino acid sequence showed significant identity to plant and mammalian serine racemases and contained conserved pyridoxal 5-phosphate (PLP)-binding lysine and PLP–interacting amino acid residues. The purified gene product catalyzed not only racemization of serine but also dehydration of serine to pyruvate. The enzyme requires PLP and divalent cations such as Ca2+, Mg2+, or Mn2+, but not ATP, whereas mammalian serine racemase activity is increased by ATP. In addition to the results regarding the effect of ATP on enzyme activity and the phylogenetic analysis of eukaryotic serine racemases, the antiserum against Arabidopsis serine racemase did not form a precipitate with barley and rice serine racemases. This suggests that plant serine racemases represent a distinct group in the eukaryotic serine racemase family and can be clustered into monocot and dicot types. |
Keywords | Hordeum vulgare L.
Oryza sativa
Gramineae
Pyridoxal 5-phosphate
Serine racemase
Serine dehydratase
d-Amino acid
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Note | Digital Object Identifier:10.1016/j.phytochem.2007.03.040
Published with permission from the copyright holder. This is the institute's copy, as published in PHYTOCHEMISTRY, June 2007, Volume 68, Issue 11, Pages 1530-1536.
Publisher URL:http://dx.doi.org/10.1016/j.phytochem.2007.03.040
Direct access to Thomson Web of Science record
Copyright © 2007 Elsevier B. V. All rights reserved.
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Published Date | 2007-6
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Publication Title |
PHYTOCHEMISTRY
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Volume | volume68
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Issue | issue11
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Start Page | 1530
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End Page | 1536
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Content Type |
Journal Article
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language |
English
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Refereed |
True
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DOI | |
Submission Path | biochemistry/5
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