Although part of the coenzyme A pathway, vanin 1 (also known as pantetheinase) sits on the cell surface of many cell types as an ectoenzyme, catalyzing the breakdown of pantetheine to pantothenic acid (vitamin B₅) and cysteamine, a strong reducing agent. Vanin 1 was initially discovered as a protein involved in the homing of leukocytes to the thymus. Numerous studies have shown that vanin 1 is involved in inflammation, and more recent studies have shown a key role in metabolic disease. Here, the X‐ray crystal structure of human vanin 1 at 2.25 Å resolution is presented, which is the first reported structure from the vanin family, as well as a crystal structure of vanin 1 bound to a specific inhibitor. These structures illuminate how vanin 1 can mediate its biological roles by way of both enzymatic activity and protein–protein interactions. Furthermore, it sheds light on how the enzymatic activity is regulated by a novel allosteric mechanism at a domain interface.

中文翻译：

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Vanin 1的结构：连接代谢性疾病和炎症的关键酶。

尽管辅酶A途径的一部分，但范宁1（也称为泛酸酶）作为一种外切酶位于许多细胞类型的细胞表面，催化泛酸分解为泛酸（维生素B ₅）和半胱胺，一种强还原剂。最初发现Vanin 1是一种涉及白细胞归巢至胸腺的蛋白质。大量研究表明，vanin 1与炎症有关，而最近的研究表明，vanin 1在代谢疾病中起关键作用。在这里，以2.25Å的分辨率显示了人类Vanin 1的X射线晶体结构，这是Vanin家族中第一个报道的结构，也是与特定抑制剂结合的Vanin 1的晶体结构。这些结构阐明了Vanin 1如何通过酶促活性和蛋白质-蛋白质相互作用来介导其生物学作用。此外，它揭示了如何在域界面上通过新颖的变构机制调节酶活性。