Trifluorosubstrates as mechanistic probes for an FMN-dependent l-2-hydroxy acid-oxidizing enzyme
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- 作者：Florence Lederera ; b ; florence.lederer@u-psud.fr" class="auth_mail" title="E-mail the corresponding author ; Caroline Vignauda ; 1 ; Paul Northa ; Sabrina Bodevina
- 关键词：DCIP ; dichlorophenol indophenol ; Fcb2 ; Flavocytochrome b2 ; FDH ; Fcb2 flavodehydrogenase domain ; F1Pyr ; monofluoropyruvate ; F1Lac ; monofluorolactate ; F3Pyr ; trifluoropyruvate ; F3Lac ; trifluorolactate ; LCHAO ; long chain hydroxy acid oxidase ; LDH ; NAD-dependent lactate dehydrogenase ; LMO ; lactate monooxygenase ; MDH ; mandelate dehydrogenase
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：September 2016
- 年：2016
- 卷：1864
- 期：9
- 页码：1215-1221
- 全文大小：582 K
文摘
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Trifluorolactate is a substrate for an FMN-dependent lactate dehydrogenase (LDH).
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Trifluorolactate is known to be an inhibitor for an NAD-dependent LDH.
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Trifluoropyruvate reoxidizes the reduced FMN-dependent LDH faster than pyruvate.
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Trifluoropyruvate is reduced more slowly than pyruvate by the NAD-dependent LDH.
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The chemical mechanism of the FMN-dependent and NAD-dependent LDH's is different.