Rafice Sara A, Chauhan Nishma, Efimov Igor, Basran Jaswir, Raven Emma Lloyd
Department of Chemistry, University of Leicester, University Road, Leicester, UK.
Biochem Soc Trans. 2009 Apr;37(Pt 2):408-12. doi: 10.1042/BST0370408.
The family of haem dioxygenases catalyse the initial oxidative cleavage of L-tryptophan to N-formylkynurenine, which is the first, rate-limiting, step in the L-kynurenine pathway. In the present paper, we discuss and compare structure and function across the family of haem dioxygenases by focusing on TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase), including a review of recent structural information for both enzymes. The present paper describes how the recent development of recombinant expression systems has informed our more detailed understanding of the substrate binding, catalytic activity and mechanistic properties of these haem dioxygenases.
血红素双加氧酶家族催化L-色氨酸初步氧化裂解生成N-甲酰犬尿氨酸,这是L-犬尿氨酸途径中的第一步,也是限速步骤。在本文中,我们通过聚焦色氨酸2,3-双加氧酶(TDO)和吲哚胺2,3-双加氧酶(IDO)来讨论和比较血红素双加氧酶家族的结构与功能,包括对这两种酶近期结构信息的综述。本文描述了重组表达系统的最新进展如何使我们对这些血红素双加氧酶的底物结合、催化活性和机制特性有了更详细的了解。