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The methylglutaconyl-CoA hydratase, mitochondrial protein binds to the AU-rich element (ARE), a common element found in the 3' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. Additionally we are shipping AU RNA Binding Protein/enoyl-CoA Hydratase Antibodies (32) and and many more products for this protein.
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These findings implicate Agmat in the depressive-like phenotype of Crtc1 (show CRTC1 Proteins)(-/-) mice, refine current understanding of the agmatinergic system in the brain and highlight its putative role in major depression.
It thus appears that mammalian AGMs form a distinct group within the family of ureahydrolases that (i) either fold in a manner distinct from other members in this family, or (ii) require accessory proteins to bind Mn(2+) in a mechanism related to that observed for the Ni(2+)-dependent urease.
AUH localizes to the inner mitochondrial membrane and matrix where it associates with mitochondrial ribosomes and regulates protein synthesis.
Phenotypic heterogeneity in two siblings with 3-methylglutaconic aciduria type I caused by a novel deletion of exons 1-3 within the AUH gene.
3-Methylglutaconic aciduria type I is caused by mutations in AUH
Human 3-methylglutaconyl-CoA hydratase is identical with RNA-binding protein (show PTBP1 Proteins) (AUH); molecular analyses of MGA1 (show CUBN Proteins) patients show homozygosity or compound heterozygosity for mutations in AUH.
Mutation analysis in the AUH gene revealed homozygosity for a novel splice site mutation IVS9-2A>G. We conclude that MGA1 (show CUBN Proteins) may be associated with fever-associated seizures even in children without delayed psychomotor development.
Mutations in the AUH gene are linked to metabolic disease 3-methylglutaconic aciduria type I (MGA1 (show CUBN Proteins)).
The AUH trimer dimerizes upon binding to one molecule of a long RNA containing 24 repeats of the AUUU motif, (AUUU)(24)A.
The methylglutaconyl-CoA hydratase, mitochondrial protein binds to the AU-rich element (ARE), a common element found in the 3' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. ARE elements are involved in directing RNA to rapid degradation and deadenylation. AUH is also homologous to enol-CoA hydratase, an enzyme involved in fatty acid degradation, and has been shown to have intrinsic hydratase enzymatic activity. AUH is thus a bifunctional chimera between RNA binding and metabolic enzyme activity. A possible subcellular localization in the mitochondria has been demonstrated for the mouse homolog of this protein which shares 92% identity with the human protein. It has been suggested that AUH may have a novel role as a mitochondrial located AU-binding protein. Human AUH is expressed as a single mRNA species of 1.8 kb, and translated as a 40-kDa precursor protein which is subsequently processed to a 32-kDa mature form.
AU RNA binding protein/enoyl-coenzyme A hydratase
, methylglutaconyl-CoA hydratase, mitochondrial
, agmatinase, mitochondrial
, AU RNA binding protein/enoyl-Coenzyme A hydratase
, 3-methylglutaconyl-CoA hydratase
, AU RNA-binding protein/enoyl-Coenzyme A hydratase
, AU-binding protein/Enoyl-CoA hydratase
, AU-specific RNA-binding enoyl-CoA hydratase
, AU-binding enoyl-CoA hydratase