title: 4-Hydroxyphenylpyruvate dioxygenase and hydroxymandelate synthase: exemplars of the α-keto acid dependent oxygenases.
abstract: 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.
authors.affiliation: Department of Chemistry and Biochemistry, University of Wisconsin-Milwaukee, 3210 N. Cramer St, Milwaukee, WI 53211-3209, United States. Electronic address: moran@uwm.edu.
authors.forename: Graham R
authors.initials: GR
authors.lastname: Moran
mesh_terms: D015111:4-Hydroxyphenylpyruvate Dioxygenase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001419:Bacteria / Q000737:chemistry / Q000201:enzymology; D049308:Dioxygenases / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008333:Mandelic Acids / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D013379:Substrate Specificity
chemical_list: D008333:Mandelic Acids; D049308:Dioxygenases; D015111:4-Hydroxyphenylpyruvate Dioxygenase
keywords: 4-Hydroxyphenylpyruvate dioxygenase; Dioxygenase; Ferrous; Hydroxymandelate synthase; Molecular oxygen; Oxygenase; α-Keto acid