کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1925232 | 1536355 | 2014 | 11 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: 4-Hydroxyphenylpyruvate dioxygenase and hydroxymandelate synthase: Exemplars of the α-keto acid dependent oxygenases 4-Hydroxyphenylpyruvate dioxygenase and hydroxymandelate synthase: Exemplars of the α-keto acid dependent oxygenases](/preview/png/1925232.png)
• The function, structure, and chemistry of HPPD and HMS are described.
• HPPD and HMS offer unique insights into α-keto acid dependent dioxygenase chemistry.
• The chemistry and relevance of HPPD inhibition is described in detail.
4-Hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS) are outliers within the α-keto acid dependent oxygenase (αKAO) family. HPPD and HMS catalyze the chemistry of the majority of enzymes within the αKAO family but are clearly mechanistically convergent, having a grossly different structural topology. Some of the unique characteristics of HPPD and HMS have elucidated select parts of the catalytic cycle that are obscured in other family members. Moreover, the inhibitory chemistry of HPPD is a phenomenon with ever-expanding relevance across all kingdoms of life. This review is a synopsis of the literature pertaining to HPPD and HMS. It is not intended as an exhaustive compilation of all observations made for these enzymes but rather a condensed narrative that connects those studies that have advanced the understanding of the chemistry of both enzymes.
Journal: Archives of Biochemistry and Biophysics - Volume 544, 15 February 2014, Pages 58–68