Format

Send to

Choose Destination
J Biol Chem. 2015 Mar 13;290(11):6755-62. doi: 10.1074/jbc.M114.609305. Epub 2015 Jan 9.

Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase.

Author information

1
From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and.
2
the Institute for General, Inorganic and Theoretical Chemistry and Center for Molecular Biosciences Innsbruck, Universität Innsbruck, Innrain 80-82, 6020 Innsbruck, Austria.
3
From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and pidder.jansen-duerr@uibk.ac.at.

Abstract

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.

KEYWORDS:

Computer Modeling; Decarboxylase; Energy Metabolism; FAH Domain; FAHD1; Mitochondria; Oxaloacetate Decarboxylase; Pyruvate

PMID:
25575590
PMCID:
PMC4358102
DOI:
10.1074/jbc.M114.609305
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center