Institute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria.
acib - Austrian Center of Industrial Biotechnology, Krenngasse 37, 8010, Graz, Austria.
Chembiochem. 2024 Apr 16;25(8):e202400121. doi: 10.1002/cbic.202400121. Epub 2024 Mar 8.
Carboxylic acid reductase enzymes (CARs) are well known for the reduction of a wide range of carboxylic acids to the respective aldehydes. One of the essential CAR domains - the reductase domain (R-domain) - was recently shown to catalyze the standalone reduction of carbonyls, including aldehydes, which are typically considered to be the final product of carboxylic acid reduction by CAR. We discovered that the respective full-length CARs were equally able to reduce aldehydes. Herein we aimed to shed light on the impact of this activity on aldehyde production and acid reduction in general. Our data explains previously inexplicable results and a new CAR from Mycolicibacterium wolinskyi is presented.
羧酸还原酶（CAR）酶以还原广泛的羧酸为相应醛而闻名。最近发现，其中一个重要的 CAR 结构域 - 还原酶结构域（R 结构域） - 可以单独催化羰基的还原，包括通常被认为是 CAR 还原羧酸的最终产物的醛。我们发现相应的全长 CAR 也能够还原醛。本文旨在阐明这种活性对醛的产生和一般酸还原的影响。我们的数据解释了以前无法解释的结果，并介绍了来自 Mycolicibacterium wolinskyi 的一种新的 CAR。
