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首页> 外文期刊>FEBS Open Bio >Identification and characterization of trans-3-hydroxy-l-proline dehydratase and @D^1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-l-proline metabolism of bacteria
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Identification and characterization of trans-3-hydroxy-l-proline dehydratase and @D^1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-l-proline metabolism of bacteria

机译：反式-3-羟基-1-脯氨酸脱水酶和@ D ^ 1-吡咯啉-2-羧酸还原酶参与细菌反式-3-羟基-1-脯氨酸代谢的鉴定与表征

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trans-4-Hydroxy-l-proline (T4LHyp) and trans-3-hydroxy-l-proline (T3LHyp) occur mainly in collagen. A few bacteria can convert T4LHyp to @a-ketoglutarate, and we previously revealed a hypothetical pathway consisting of four enzymes at the molecular level (J Biol Chem (2007) 282, 6685-6695; J Biol Chem (2012) 287, 32674-32688). Here, we first found that Azospirillum brasilense has the ability to grow not only on T4LHyp but also T3LHyp as a sole carbon source. In A. brasilense cells, T3LHyp dehydratase and NAD(P)H-dependent @D^1-pyrroline-2-carboxylate (Pyr2C) reductase activities were induced by T3LHyp (and d-proline and d-lysine) but not T4LHyp, and no effect of T3LHyp was observed on the expression of T4LHyp metabolizing enzymes: a hypothetical pathway of T3LHyp->Pyr2C->l-proline was proposed. Bacterial T3LHyp dehydratase, encoded to LhpH gene, was homologous with the mammalian enzyme. On the other hand, Pyr2C reductase encoded to LhpI gene was a novel member of ornithine cyclodeaminase/@m-crystallin superfamily, differing from known bacterial protein. Furthermore, the LhpI enzymes of A. brasilense and another bacterium showed several different properties, including substrate and coenzyme specificities. T3LHyp was converted to proline by the purified LhpH and LhpI proteins. Furthermore, disruption of LhpI gene from A. brasilense led to loss of growth on T3LHyp, d-proline and d-lysine, indicating that this gene has dual metabolic functions as a reductase for Pyr2C and @D^1-piperidine-2-carboxylate in these pathways, and that the T3LHyp pathway is not linked to T4LHyp and l-proline metabolism.
机译：反式-4-羟基-1-脯氨酸（T4LHyp）和反式-3-羟基-1-脯氨酸（T3LHyp）主要存在于胶原蛋白中。少数细菌可以将T4LHyp转化为α-酮戊二酸，我们先前揭示了一种在分子水平上由四种酶组成的假想途径（J Biol Chem（2007）282，6685-6695; J Biol Chem（2012）287，32674- 32688）。在这里，我们首先发现，巴西拟螺旋藻不仅可以在T4LHyp上生长，而且还可以在T3LHyp上作为唯一碳源生长。在巴西拟南芥细胞中，T3LHyp（以及d-脯氨酸和d-赖氨酸）诱导了T3LHyp脱水酶和NAD（P）H依赖的@ D ^ 1-吡咯啉-2-羧酸（Pyr2C）还原酶活性，但不诱导T4LHyp，并且没有观察到T3LHyp对T4LHyp代谢酶表达的影响：提出了T3LHyp-> Pyr2C-> 1-脯氨酸的假设途径。编码为LhpH基因的细菌T3LHyp脱水酶与哺乳动物酶同源。另一方面，编码为LhpI基因的Pyr2C还原酶是鸟氨酸环脱氨酶/ m-crystallin超家族的新成员，与已知的细菌蛋白不同。此外，巴西农杆菌和另一种细菌的LhpI酶表现出几种不同的特性，包括底物和辅酶特异性。通过纯化的LhpH和LhpI蛋白将T3LHyp转化为脯氨酸。此外，来自巴西农杆菌的LhpI基因的破坏导致T3LHyp，d-脯氨酸和d-赖氨酸的生长损失，表明该基因具有双重代谢功能，作为Pyr2C和@ D ^ 1-哌啶-2-羧酸的还原酶。在这些途径中，T3LHyp途径与T4LHyp和L-脯氨酸代谢没有联系。

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