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論文
- タイトル
- タイトル（英）
- A new branch of mammalian vitamin B6 metabolism: AKR1C-mediated conversion of pyridoxal to pyridoxine and 4-pyridoxolactone.
- 参照URL
- https://researchmap.jp/toriumi1207/published_papers/52198037
- 著者
- 著者（英）
- Nayu Kito,Yasuyuki Kitaura,Kyoka Iino,Kazuya Toriumi,Hyunah Noh,Naoya Ogawa,Makoto Arai,Hisashi Hemmi,Tomokazu Ito
- 担当区分
- 概要
- 概要（英）
- Pyridoxal 5'-phosphate (PLP), the coenzyme form of vitamin B6, is indispensable for diverse metabolic processes, especially amino acid metabolism. In mammals, PLP is primarily synthesized via a salvage pathway involving pyridoxal kinase (PLK), pyridoxine/pyridoxamine 5'-phosphate oxidase (PNPO), and pyridoxal phosphate phosphatase (PLPP). However, recent evidence suggests the presence of additional, yet unidentified, enzymatic contributors to this pathway. Here, we identify aldo-keto reductase family 1 member C (AKR1C) isozymes as previously unrecognized enzymes involved in vitamin B6 metabolism. We demonstrate that AKR1Cs catalyze two novel reactions: an NADPH-dependent pyridoxal reductase (PLR) activity that converts pyridoxal (PL) to pyridoxine (PN), and an NADP+-dependent pyridoxal dehydrogenase (PLD) activity that oxidizes PL to 4-pyridoxolactone (4-PLA). Both reactions occur under physiological conditions and significantly impact intracellular vitamin B6 vitamer profiles. Moreover, we show that elevated PL levels suppress AKR1C activities toward non-B6 substrates, indicating reciprocal cross-talk between vitamin B6 metabolism and other AKR1C-dependent metabolic processes. This study expands the current framework of mammalian vitamin B6 metabolism, highlighting AKR1Cs as metabolic hubs with broad regulatory implications.
- 出版者・発行元
- 出版者・発行元（英）
- 誌名
- 誌名（英）
- The FEBS journal
- 巻
- 号
- 開始ページ
- 終了ページ
- 出版年月
- 2026年2月25日
- 査読の有無
- 査読有り
- 招待の有無
- 掲載種別
- 研究論文（学術雑誌）
- ISSN
- DOI URL
- https://doi.org/10.1111/febs.70471
- 共同研究・競争的資金等の研究課題
研究者
鳥海 和也
(トリウミ カズヤ)