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  1. B300 農学部/生命農学研究科
  2. B300a 雑誌掲載論文
  3. 学術雑誌

Suicide substrate reaction-like modification of mouse serine racemase with L-serine

http://hdl.handle.net/2237/0002013898
http://hdl.handle.net/2237/0002013898
fa7ba442-aa6e-4361-959b-90adf21788a6
名前 / ファイル ライセンス アクション
JB_177_6_437.pdf JB_177_6_437.pdf (1.4 MB)
 Download is available from 2026/6/1.
アイテムタイプ itemtype_ver1(1)
公開日 2026-01-29
タイトル
タイトル Suicide substrate reaction-like modification of mouse serine racemase with L-serine
言語 en
著者 Hata, Akari

× Hata, Akari

en Hata, Akari

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Ito, Tomokazu

× Ito, Tomokazu

en Ito, Tomokazu

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Mori, Hitoshi

× Mori, Hitoshi

en Mori, Hitoshi

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Ogawa, Takuya

× Ogawa, Takuya

en Ogawa, Takuya

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Kurihara, Tatsuo

× Kurihara, Tatsuo

en Kurihara, Tatsuo

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Hemmi, Hisashi

× Hemmi, Hisashi

en Hemmi, Hisashi

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Yoshimura, Tohru

× Yoshimura, Tohru

en Yoshimura, Tohru

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アクセス権
アクセス権 embargoed access
アクセス権URI http://purl.org/coar/access_right/c_f1cf
権利
権利情報 This is a pre-copyedited, author-produced version of an article accepted for publication in [Journal of biochemistry] following peer review. The version of record [Akari Hata, Tomokazu Ito, Hitoshi Mori, Takuya Ogawa, Tatsuo Kurihara, Hisashi Hemmi, Tohru Yoshimura, Suicide substrate reaction-like modification of mouse serine racemase with L-serine, The Journal of Biochemistry, Volume 177, Issue 6, June 2025, Pages 437–445, https://doi.org/10.1093/jb/mvaf019] is available online at: https://doi.org/10.1093/jb/mvaf019.
言語 en
内容記述
内容記述タイプ Abstract
内容記述 A pyridoxal 5’-phosphate-dependent fold-type II serine racemase (SR) is responsible for the synthesis of D-Ser, which serves as a co-agonist of N-methyl-D-aspartate glutamate receptor. In addition to racemization, SR catalyzes the dehydration of D- and L-Ser. SR is suggested to be involved in the D-Ser degradation in vivo, but this has not been confirmed. In this study, we found that mouse SR (mSR) underwent a suicide substrate reaction-like modification with its substrate, resulting in a remarkable change in its reaction specificity. mSR gradually lost its activity by the incubation with L- and D-Ser, but not completely. mSR was labelled with [14C]-L-Ser. ESI-MS analysis revealed that the molecular mass of SR increased by 84 Da by the incubation with L-Ser. Taken together with the results of previous crystallographic studies of fission yeast SR, we concluded that the active site lysine residue of mSR was modified with an α-aminoacrylate intermediate generated from L-Ser and converted to a lysinoalanine residue. The modification significantly decreased the racemization and L-Ser dehydration activities, while dramatically increased the D-Ser dehydration activity by the ~100 times reduction of the Km value. This is probably advantageous for the D-Ser degradation by mSR under physiological conditions.
言語 en
出版者
出版者 Oxford University Press
言語 en
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
関連情報
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1093/jb/mvaf019
収録物識別子
収録物識別子タイプ PISSN
収録物識別子 0021-924X
書誌情報 en : Journal of biochemistry

巻 177, 号 6, p. 437-445, 発行日 2025-06
ファイル公開日
日付 2026-06-01
日付タイプ Available
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