脯氨酸分解代谢的结构生物学
Structural biology of proline catabolism.
作者信息
Tanner John J
机构信息
Departments of Chemistry and Biochemistry, University of Missouri, Columbia, MO 65211, USA.
出版信息
Amino Acids. 2008 Nov;35(4):719-30. doi: 10.1007/s00726-008-0062-5. Epub 2008 Mar 28.
Abstract
The proline catabolic enzymes proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase catalyze the 4-electron oxidation of proline to glutamate. These enzymes play important roles in cellular redox control, superoxide generation, apoptosis and cancer. In some bacteria, the two enzymes are fused into the bifunctional enzyme, proline utilization A. Here we review the three-dimensional structural information that is currently available for proline catabolic enzymes. Crystal structures have been determined for bacterial monofunctional proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase, as well as the proline dehydrogenase and DNA-binding domains of proline utilization A. Some of the functional insights provided by analyses of these structures are discussed, including substrate recognition, catalytic mechanism, biochemical basis of inherited proline catabolic disorders and DNA recognition by proline utilization A.
摘要
脯氨酸分解代谢酶脯氨酸脱氢酶和Δ¹-吡咯啉-5-羧酸脱氢酶催化脯氨酸的4电子氧化生成谷氨酸。这些酶在细胞氧化还原控制、超氧化物生成、细胞凋亡和癌症中发挥重要作用。在一些细菌中，这两种酶融合成双功能酶——脯氨酸利用A。本文综述了目前可获得的脯氨酸分解代谢酶的三维结构信息。已确定了细菌单功能脯氨酸脱氢酶和Δ¹-吡咯啉-5-羧酸脱氢酶以及脯氨酸利用A的脯氨酸脱氢酶和DNA结合结构域的晶体结构。讨论了对这些结构分析所提供的一些功能见解，包括底物识别、催化机制、遗传性脯氨酸分解代谢障碍的生化基础以及脯氨酸利用A对DNA的识别。
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