Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic Gene Ontology annotation based on Rhea mapping
Combined Automated Annotation using Multiple IEA Methods
Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids.
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Using recombinant human L-bifunctional protein (LBP) and patient fibroblasts, shows that peroxisomes (not mitochondria) beta-oxidize C16 dicarboxylic acid and that LBP is one of the main enzymes involved; first demonstration of a specific physiological function for LBP.
"the main enzymes involved in
beta-oxidation of C16DCA are SCOX, both LBP and DBP"
Import of human bifunctional enzyme into peroxisomes of human hepatoma cells in vitro.
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The C-terminal SKL tripeptide is the peroxisomal targeting signal (PTS1) directing import of the human bifunctional enzyme; deletion of the last nine residues prevents import.
"SKL, located at the carboxyl-terminus of human bifunctional
enzyme appears to be the targeting signal"
Molecular organization of peroxisomal enzymes: protein-protein interactions in the membrane and in the matrix.
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Yeast two-hybrid, affinity purification and co-immunoprecipitation show that catalase physically interacts with L-bifunctional enzyme (EHHADH), which may help localize catalase at the peroxisomal H2O2 production site.
"catalase physically
interacts with L-bifunctional enzyme (L-BFE)"
A proteome-scale map of the human interactome network.
Immunocytochemical demonstration of peroxisomal enzymes in human kidney biopsies.
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Immunocytochemistry localizes the bifunctional protein (enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase) to peroxisomes of human kidney proximal tubular epithelial cells.
"bifunctional protein
(enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase)"
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
A proteome-scale map of the SARS-CoV-2-human contactome.
Multimodal cell maps as a foundation for structural and functional genomics.
cDNA cloning of the human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme and localization to chromosome 3q26.3-3q28: a free left Alu Arm is inserted in the 3' noncoding region.
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Reports the full-length human cDNA for the peroxisomal enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme (chromosome 3q26.3-3q28); the enzyme is one of the four peroxisomal beta-oxidation enzymes, carries a C-terminal SKL PTS1 signal, and is expressed most strongly in liver and kidney.
"one
of the four enzymes of the peroxisomal beta-oxidation pathway"
Immunocytochemical localization of peroxisomal proteins in human liver and kidney.
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Immunocytochemistry localizes the three peroxisomal beta-oxidation enzymes (including the bifunctional protein) to peroxisomes in human liver.
"subcellular localization of peroxisomal proteins (catalase, the
three beta-oxidation enzymes"
Beta-oxidation of very long chain fatty acids
EHHADH hydrates trans-2,3-dehydrohexacosanoyl-CoA
EHHADH dehydrogenates 3-hydroxyhexacosanoyl-CoA
Cargo of PEX5S,L translocates from the cytosol to the peroxisomal matrix
PEX5S,L:Cargo binds PEX13:PEX14:PEX2:PEX10:PEX12 (Docking and Translocation Module)