隐球菌UJ1 d -天冬氨酸氧化酶的晶体结构。

IF 1.1 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Acta crystallographica. Section F, Structural biology communications Pub Date : 2025-09-19 DOI:10.1107/S2053230X25008192

Masaru Goto, Risako Nonaka, Taichi Mizobuchi, Daiki Imanishi, Shouji Takahashi

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引用次数: 0

摘要

d -天冬氨酸氧化酶（DDO）利用辅酶黄素腺嘌呤二核苷酸氧化酸性d -氨基酸，生成相应的α-酮酸和氨。DDO不同于d -氨基酸氧化酶（DAAO），后者作用于中性和碱性d -氨基酸。虽然DDO的酶学性质已经在一些物种中被表征，但DDO的结构仍然不清楚。采用1.70 Å分辨率的x射线晶体学方法测定了humicola隐球菌菌株UJ1 （chDDO）的DDO结构。虽然已知daao的三维结构是同型二聚体，但chDDO形成了同型四聚体。发现这种差异是由一个环的删除和两个环的插入引起的。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Crystal structure of d-aspartate oxidase from Cryptococcus humicola UJ1

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Crystal structure of d-aspartate oxidase from Cryptococcus humicola UJ1

The enzyme d-aspartate oxidase (DDO) oxidizes acidic d-amino acids using the coenzyme flavin adenine dinucleotide to generate the corresponding α-keto acids and ammonia. DDO differs from d-amino-acid oxidase (DAAO), which acts on neutral and basic d-amino acids. Although the enzymatic properties of DDO have been characterized in several species, the structure of DDO had remained unclear. The structure of DDO derived from Cryptococcus humicola strain UJ1 (chDDO) was determined by X-ray crystallography at 1.70 Å resolution. While the three-dimensional structures of DAAOs are known to be homodimers, chDDO forms a homotetramer. This difference was found to be caused by the deletion of one loop and the insertion of two loops.

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来源期刊

Acta crystallographica. Section F, Structural biology communications BIOCHEMICAL RESEARCH METHODSBIOCHEMISTRY &-BIOCHEMISTRY & MOLECULAR BIOLOGY

CiteScore

1.90

自引率

0.00%

发文量

期刊介绍： Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.