First Author | Pircher H | Year | 2015 |
Journal | J Biol Chem | Volume | 290 |
Issue | 11 | Pages | 6755-62 |
PubMed ID | 25575590 | Mgi Jnum | J:278569 |
Mgi Id | MGI:6356505 | Doi | 10.1074/jbc.M114.609305 |
Citation | Pircher H, et al. (2015) Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase. J Biol Chem 290(11):6755-62 |
abstractText | Fumarylacetoacetate hydrolase (FAH) domain-containing proteins occur in both prokaryotes and eukaryotes, where they carry out diverse enzymatic reactions, probably related to structural differences in their respective FAH domains; however, the precise relationship between structure of the FAH domain and the associated enzyme function remains elusive. In mammals, three FAH domain-containing proteins, FAHD1, FAHD2A, and FAHD2B, are known; however, their enzymatic function, if any, remains to be demonstrated. In bacteria, oxaloacetate is subject to enzymatic decarboxylation; however, oxaloacetate decarboxylases (ODx) were so far not identified in eukaryotes. Based on molecular modeling and subsequent biochemical investigations, we identified FAHD1 as a eukaryotic ODx enzyme. The results presented here indicate that dedicated oxaloacetate decarboxylases exist in eukaryotes. |