Disease relevance of AUH

• By heterologous expression in Escherichia coli, we show that 3-methylglutaconyl-CoA hydratase is encoded by the AUH gene, whose product had been reported elsewhere as an AU-specific RNA-binding protein [1].

High impact information on AUH

• Thus, this gene, designated AUH, encodes an RNA binding protein with intrinsic enzymatic activity [2].
• It was further determined, using immunoelectron microscopy, that AUH is located in the mitochondria of mouse cells [3].
• All murine cells studied contained a single AUH transcript of approx. 1.7kb and an investigation of tissue-specific expression revealed highest levels in kidney, skeletal muscle, heart, liver and spleen [3].
• AUH exhibited dual activities, namely A+U-specific RNA-binding and catalytic activity as enoyl-CoA hydratase [4].
• A mutational analysis showed that the lysine residues in alpha helix H1 are essential to the RNA binding activity of AUH [5].

Biological context of AUH

• The boy is homozygous for an N-terminal frameshift mutation in the AUH gene [6].

Anatomical context of AUH

• Based on these results, a new assay for AUH activity in fibroblast homogenates was developed [7].

Associations of AUH with chemical compounds

• Complete absence of 3-methylglutaconyl-CoA hydratase/AUH appears to be compatible with normal development in some cases [6].
• Here we present kinetic data of the purified gene product of AUH using different CoA-substrates [7].
• The best substrates were (E)-3-MG-CoA (V(max) = 3.9 U.mg(-1), K(m) = 8.3 microm, k(cat) = 5.1 s(-1)) and (E)-glutaconyl-CoA (V(max) = 1.1 U.mg(-1), K(m) = 2.4 microm, k(cat) = 1.4 s(-1)) giving strong evidence that the AUH gene encodes for the major human 3-MG-CoA hydratase in leucine degradation [7].
• Sixty five (82%) of the 79 WI strains were typed as being serovar Aedgkih, and 47 (72%) of these strains required arginine, uracil, and hypoxanthine for growth (AUH-) [8].

Physical interactions of AUH

• The human AUH gene has been reported to encode for a bifunctional enzyme with both RNA-binding and enoyl-CoA-hydratase activity [7].

References