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


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.

SUBMITTER: Pircher H 

PROVIDER: S-EPMC4358102 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature

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

Pircher Haymo H   von Grafenstein Susanne S   Diener Thomas T   Metzger Christina C   Albertini Eva E   Taferner Andrea A   Unterluggauer Hermann H   Kramer Christian C   Liedl Klaus R KR   Jansen-Dürr Pidder P  

The Journal of biological chemistry 20150109 11


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 de  ...[more]

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