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Literature summary extracted from

  • Yang, S.Y.; He, X.Y.; Schulz, H.
    3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease (2005), FEBS J., 272, 4874-4883.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.35 pharmacology the short-chain 3-hydroxyacyl-CoA dehydrogenase is a target for intervention in case of Alzheimer's disease and Parkinson's disease Homo sapiens
1.1.1.178 medicine important in brain development and aging, SCHAD deficiency is an inherited defect in mitochondrial fatty acid oxidation, reported cases of SCHAD deficiency are actually due to a deficiency of HAD, abnormal levels may contribute to the pathogenesis of some neural disorders, potential target for intervention in Alzheimer's disease, Parkinson's disease, and an X-linked mental retardation Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.178
-
 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.178 L122V affects brain development and brain function in patients Homo sapiens
1.1.1.178 R130C affects brain development and brain function in patients Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.178 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone specific inhibitor of SCHAD, forms a covalent adduct with NAD+ by a catalytic suicide mechanism Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.35 mitochondrion
-
 Sus scrofa 5739
-
1.1.1.35 mitochondrion
-
 Homo sapiens 5739
-
1.1.1.178 mitochondrion
-
 Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.35 additional information Homo sapiens the enzyme is essentially involved in mitochondrial fatty acid beta-oxidation by catalyzing straight chain 3-hydroxyacyl-CoAs, the enzyme plays a role in Alzheimer's disease and Parkinson's disease, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.35 Homo sapiens Q16836
-
-
1.1.1.35 Sus scrofa
-
-
-
1.1.1.178 Homo sapiens
-
-
-
1.1.1.178 Mus musculus
-
-
-
1.1.1.178 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.178
-
 Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.35 (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+ molecular reaction mechanism, a His-Glu pair is essential for actalysis in the active site Sus scrofa
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.35 heart
-
 Sus scrofa
-
1.1.1.178 amygdala
-
 Homo sapiens
-
1.1.1.178 brain expressed in different regions Homo sapiens
-
1.1.1.178 brain levels of SCHAD/HADII are significantly reduced in the ventral midbrain of a Parkinson’s disease mouse model Mus musculus
-
1.1.1.178 cerebral cortex
-
 Homo sapiens
-
1.1.1.178 hippocampus
-
 Homo sapiens
-
1.1.1.178 hypothalamus
-
 Homo sapiens
-
1.1.1.178 liver
-
 Homo sapiens
-
1.1.1.178 liver
-
 Rattus norvegicus
-
1.1.1.178 spinal cord
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.35 3-hydroxy-2-methylacyl-CoA + NAD+ preferred substrate of SCHAD, no activity towards 3-hydroxy-2-methylacyl-CoA by HAD Sus scrofa 3-oxo-2-methylacyl-CoA + NADH
-
 ?
1.1.1.35 additional information the enzyme is essentially involved in mitochondrial fatty acid beta-oxidation by catalyzing straight chain 3-hydroxyacyl-CoAs, the enzyme plays a role in Alzheimer's disease and Parkinson's disease, overview Homo sapiens ?
-
 ?
1.1.1.35 additional information short-chain L-3-hydroxyacyl-CoA dehydrogenase shows a wide substrate spectrum including cholic acids, steroids, and fatty acids with a preference for short-chain methyl-branched acyl-CoAs, SCHAD might be identical with 17beta-hydroxysteroid dehyxrogenase in human mitochondria, overview Homo sapiens ?
-
 ?
1.1.1.35 tiglyl-CoA + NAD+ activity of SCHAD Sus scrofa 3-oxo-2-methylacyl-CoA + NADH
-
 ?
1.1.1.178 2-methyl-3-hydroxybutyryl-CoA among the best substrates Rattus norvegicus 2-methyl-acetoacetyl-CoA
-
 ?
1.1.1.178 additional information acts on a wide spectrum of substrates, including steroids, cholic acids, and fatty acids, with a preference for short chain methyl-branched acyl-CoAs Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.35 More primary structure analysis, structure-function relationship of SCHAD, overview Sus scrofa
1.1.1.35 More structure-function relationship of SCHAD, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.1.1.35 3-hydroxyacyl-CoA dehydrogenase
-
 Sus scrofa
1.1.1.35 3-hydroxyacyl-CoA dehydrogenase
-
 Homo sapiens
1.1.1.35 SCHAD
-
 Sus scrofa
1.1.1.35 SCHAD
-
 Homo sapiens
1.1.1.35 short-chain 3-hydroxyacyl-CoA dehydrogenase
-
 Sus scrofa
1.1.1.35 short-chain 3-hydroxyacyl-CoA dehydrogenase
-
 Homo sapiens
1.1.1.178 17beta-hydroxysteroid dehydrogenase type 10
-
 Mus musculus
1.1.1.178 17beta-hydroxysteroid dehydrogenase type 10
-
 Homo sapiens
1.1.1.178 17beta-hydroxysteroid dehydrogenase type 10
-
 Rattus norvegicus
1.1.1.178 2-methyl-3-hydroxybutyryl-CoA dehydrogenase
-
 Homo sapiens
1.1.1.178 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
-
 Homo sapiens
1.1.1.178 HADII
-
 Mus musculus
1.1.1.178 HADII
-
 Rattus norvegicus
1.1.1.178 HSD10
-
 Mus musculus
1.1.1.178 HSD10
-
 Rattus norvegicus
1.1.1.178 MHBD
-
 Homo sapiens
1.1.1.178 SCHAD
-
 Mus musculus
1.1.1.178 SCHAD
-
 Homo sapiens
1.1.1.178 SCHAD
-
 Rattus norvegicus
1.1.1.178 short chain 3-hydroxyacyl-CoA dehydrogenase
-
 Mus musculus
1.1.1.178 short chain 3-hydroxyacyl-CoA dehydrogenase
-
 Homo sapiens
1.1.1.178 short chain 3-hydroxyacyl-CoA dehydrogenase
-
 Rattus norvegicus
1.1.1.178 type II 3-hydroxyacyl-CoA dehydrogenase
-
 Mus musculus
1.1.1.178 type II 3-hydroxyacyl-CoA dehydrogenase
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.35 NAD+ dependent on Sus scrofa
1.1.1.35 NAD+ dependent on Homo sapiens