Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Pedersen, C.B.; Kolvraa, S.; Kolvraa, A.; Stenbroen, V.; Kjeldsen, M.; Ensenauer, R.; Tein, I.; Matern, D.; Rinaldo, P.; Vianey-Saban, C.; Ribes, A.; Lehnert, W.; Christensen, E.; Corydon, T.J.; Andresen, B.S.; Vang, S.; Bolund, L.; Vockley, J.; Bross, P.; Gregersen, N.
    The ACADS gene variation spectrum in 114 patients with short-chain acyl-CoA dehydrogenase (SCAD) deficiency is dominated by missense variations leading to protein misfolding at the cellular level (2008), Hum. Genet., 124, 43-56.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.3.8.1 G209S mutant shows a temperature-dependent production of SCAD tetramers with reduced amounts compared to the wild type enzyme Homo sapiens
1.3.8.1 R171W mutant shows a temperature-dependent production of SCAD tetramers with reduced amounts compared to the wild type enzyme Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.1 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.8.1 fibroblast
-
 Homo sapiens
-
1.3.8.1 muscle
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.1 butyryl-CoA + electron transfer flavoprotein
-
 Homo sapiens 2-butenoyl-CoA + reduced electron transfer flavoprotein
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.8.1 tetramer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.3.8.1 SCAD
-
 Homo sapiens
1.3.8.1 short-chain acyl-CoA dehydrogenase
-
 Homo sapiens