3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease.
3-Hydroxyacyl-CoA dehydrogenase (HAD) functions in mitochondrial fatty acid beta-oxidation by catalyzing the oxidation of straight chain 3-hydroxyacyl-CoAs. HAD has a preference for medium chain substrates, whereas short chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD) acts on a wide spectrum of substrates, including steroids, cholic acids, and fatty acids, with a preference for short chain methyl-branched acyl-CoAs. Therefore, HAD should not be referred to as SCHAD. SCHAD is not a member of the HAD family, but instead, belongs to the short chain dehydrogenase/reductase superfamily. Previously reported cases of SCHAD deficiency are due to an inherited HAD deficiency. SCHAD, also known as 17beta-hydroxysteroid dehydrogenase type 10, is important in brain development and aging. Abnormal levels of SCHAD in certain brain regions may contribute to the pathogenesis of some neural disorders. The human SCHAD gene and its protein product, SCHAD, are potential targets for intervention in conditions, such as Alzheimer's disease, Parkinson's disease, and an X-linked mental retardation, that may arise from the impaired degradation of branched chain fatty acid and isoleucine.
Yang
Song-Yu
SY
Department of Neurochemistry, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, 10314, USA. yang_songyu@yahoo.com
He
Xue-Ying
XY
Schulz
Horst
H
D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000737:chemistry / Q000172:deficiency / Q000378:metabolism*; D000544:Alzheimer Disease / Q000201:enzymology* / Q000378:metabolism; D000818:Animals; D006262:Health; D006801:Humans; D008607:Intellectual Disability / Q000201:enzymology* / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism; D010300:Parkinson Disease / Q000201:enzymology* / Q000378:metabolism
D015094:3-Hydroxyacyl CoA Dehydrogenases; C108634:HSD17B10 protein, human