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裂殖酵母Dap1的血红素铁配位残基Y83是细胞色素P450功能所必需的。

Fission yeast Dap1 heme iron-coordinating residue Y83 is required for cytochromes P450 function.

作者信息

Zhao Shan, Hughes Adam L, Espenshade Peter J

机构信息

Johns Hopkins University School of Medicine, USA.

出版信息

MicroPubl Biol. 2022 Aug 23;2022. doi: 10.17912/micropub.biology.000631. eCollection 2022.

DOI:10.17912/micropub.biology.000631
PMID:36090151
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9449707/
Abstract

Fission yeast Dap1 is a heme binding protein required for cytochromes P450 activity. Here, we tested whether Dap1 axial coordination of heme iron is required for its role in the function of the cytochrome P450 enzymes, Erg5 and Erg11. Two different mutants predicted to alter iron coordination failed to rescue growth on cobalt chloride containing medium which requires Erg5 and Erg11. In addition, deletion of did not affect expression of Erg5 or Erg11. PGRMC1, a mammalian Dap1 homolog, does not require heme binding to bind and stabilize cytochromes P450. These experiments highlight important functional differences between these conserved proteins.

摘要

裂殖酵母Dap1是一种细胞色素P450活性所需的血红素结合蛋白。在此,我们测试了血红素铁的Dap1轴向配位对于其在细胞色素P450酶Erg5和Erg11功能中的作用是否必要。预测会改变铁配位的两种不同突变体无法挽救在含有需要Erg5和Erg11的氯化钴培养基上的生长。此外,删除[此处原文缺失具体内容]并不影响Erg5或Erg11的表达。哺乳动物Dap1同源物PGRMC1不需要血红素结合来结合和稳定细胞色素P450。这些实验突出了这些保守蛋白之间重要的功能差异。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/03f2/9449707/50b347e2c7a8/25789430-2022-micropub.biology.000631.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/03f2/9449707/50b347e2c7a8/25789430-2022-micropub.biology.000631.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/03f2/9449707/50b347e2c7a8/25789430-2022-micropub.biology.000631.jpg

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本文引用的文献

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J Biol Chem. 2021 Nov;297(5):101316. doi: 10.1016/j.jbc.2021.101316. Epub 2021 Oct 20.
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Cobalt chloride, a hypoxia-mimicking agent, targets sterol synthesis in the pathogenic fungus Cryptococcus neoformans.氯化钴是一种模拟缺氧的试剂,作用于致病性真菌新型隐球菌的固醇合成。
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