Biology:FAHD1
 Generic protein structure example |
Fumarylacetoacetate hydrolase domain-containing protein 1, also known as FLJ36880 protein, is an enzyme that in humans is encoded by the FAHD1 gene on chromosome 16.[1]
Structure
The FAHD1 gene encodes for a 24-kDa protein that is localized to the mitochondrion and belongs to the fumarylacetoacetate hydrolase family of proteins.[2] The structure of FAHD1 has been resolved using X-ray crystallography at 2.2-Å resolution. The overall structure is similar to the C-terminal domain of the bifunctional enzyme HpcE from Escherichia coli C, fumarylacetoacetate hydrolase from Mus musculus and to YcgM (Apc5008) from E. coli 1262.[2] A number of conserved amino acids including Asp-102 and Arg-106 of FAHD1 appear to be important for its catalytic activity.[3]
Function
The FAHD1 protein has been shown to function as an oxaloacetate decarboxylase in eukaryotes.[4] The FAHD1 protein probably also functions as an acylpyruvase, having been shown to catalyze the hydrolysis of acetylpyruvate and fumarylpyruvate in in vitro experiments.[2] Mg(2+) was required for maximal enzyme activity.[3]
References
- ↑ "Entrez Gene: FAHD1 fumarylacetoacetate hydrolase domain containing 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81889.
- ↑ 2.0 2.1 2.2 "X-ray structure of fumarylacetoacetate hydrolase family member Homo sapiens FLJ36880". Biol. Chem. 385 (10): 935–42. 2004. doi:10.1515/BC.2004.122. PMID 15551868.
- ↑ 3.0 3.1 "Identification of human fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) as a novel mitochondrial acylpyruvase". J. Biol. Chem. 286 (42): 36500–8. 2011. doi:10.1074/jbc.M111.264770. PMID 21878618.
- ↑ "Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase". J. Biol. Chem. 290 (11): 6755–62. 2015. doi:10.1074/jbc.M114.609305. PMID 25575590.
Further reading
- "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. 2001. doi:10.1101/gr.143000. PMID 11076863.
- "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16.". Hum. Mol. Genet. 10 (4): 339–52. 2001. doi:10.1093/hmg/10.4.339. PMID 11157797.
- "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. 2001. doi:10.1101/gr.GR1547R. PMID 11230166.
- "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. 2001. doi:10.1093/embo-reports/kvd058. PMID 11256614.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315–23. 2004. doi:10.1101/gr.2122004. PMID 15231747.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. 2004. doi:10.1101/gr.2576704. PMID 15489336.
- "X-ray structure of fumarylacetoacetate hydrolase family member Homo sapiens FLJ36880.". Biol. Chem. 385 (10): 935–42. 2005. doi:10.1515/BC.2004.122. PMID 15551868.
- "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415–8. 2006. doi:10.1093/nar/gkj139. PMID 16381901.
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