Aminoadipate semialdehyde dehydrogenase

Hyperlysinemia a-Aminoadipic semialdehyde dehydrogenase Seizures, mental retardation, lack of muscle tone, ataxia ... 

Most prokaryotes employ dedicated PPTs active toward specific apoprotein substrates. Fungi also utilize separate PPTs for modification of the ACPs associated with the cytosolic and mitochondrial FAS systems, as well as the a-aminoadipate reductase involved in lysine biosynthesis [8]. The former is unusual in that it is a constituent domain of the multifunctional a-subunit (Fig. 4). Surprisingly, animals appear to employ a single PPT for servicing three different apoproteins the ACP domain of the cytosolic FAS, the ACP component of the mitochondrial FAS, and the a-aminoadipate semialdehyde dehydrogenase involved in lysine catabolism. The human PPT has recently been identified and characterized (S. Smith, 2003) and its crystal structure determined in complex with Mg, CoA, and the ACP domain of the cytosolic FAS (Structural Genomics Consortium). The ACP domain is comprised of a four-helix bundle, as are the ACPs associated with type II systems. The conserved serine residue that is the site of posttranslational modification lies at the N-terminal end of helix-2 (Fig. 6B), closely juxtaposed with the pyrophosphate of CoA that is cleaved during the phosphopantetheine transfer. Helix-2 makes multiple... 

I Homocitrate synthase 2 homocitrate dehydratase 3 homoaconitate hydratase 4 homoisocitrate dehydrogenase 5 2-aminoadipate aminotransferase 6 aminoadipate semialdehyde dehydrogenase 7 saccharopine dehydrogenase (L-glutamate forming) 8 saccharopine dehydrogenase (L-lysine forming)... 

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