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Literature summary extracted from

  • Shirao, K.; Okada, S.; Tajima, G.; Tsumura, M.; Hara, K.; Yasunaga, S.; Ohtsubo, M.; Hata, I.; Sakura, N.; Shigematsu, Y.; Takihara, Y.; Kobayashi, M.
    Molecular pathogenesis of a novel mutation, G108D, in short-chain acyl-CoA dehydrogenase identified in subjects with short-chain acyl-CoA dehydrogenase deficiency (2010), Hum. Genet., 127, 619-628.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.8.1 SCAD DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes, coexpression iin HEK-293 cells, expression of fluorescent-labeled enzyme mutants in U2-OS cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.3.8.1 E344G site-directed mutagenesis, the SCAD mutant shows reduced activity compared to the wild-typ enzyme, but does not influence the wild-type SCAD activity when co-transfected in HEK-293 cells Homo sapiens
1.3.8.1 G108D site-directed mutagenesis, the SCAD mutant shows reduced activity compared to the wild-typ enzyme, but does not influence the wild-type SCAD activity when co-transfected in HEK-293 cells Homo sapiens
1.3.8.1 P55L site-directed mutagenesis, the SCAD mutant shows reduced activity compared to the wild-typ enzyme, but does not influence the wild-type SCAD activity when co-transfected in HEK-293 cells Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.8.1 mitochondrion
-
Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.8.1 butanoyl-CoA + acceptor Homo sapiens
-
but-2-enoyl-CoA + reduced acceptor
-
?
1.3.8.1 hexanoyl-CoA + acceptor Homo sapiens
-
hex-2-enoyl-CoA + reduced acceptor
-
?
1.3.8.1 pentanoyl-CoA + acceptor Homo sapiens
-
pent-2-enoyl-CoA + reduced acceptor
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.1 Homo sapiens D4QEZ8
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.8.1 fibroblast
-
Homo sapiens
-
1.3.8.1 HEK-293 cell
-
Homo sapiens
-
1.3.8.1 lymphocyte
-
Homo sapiens
-
1.3.8.1 additional information SCAD activity levels in different tissues vary greatly, immunohistochemic analysis, overview 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 butanoyl-CoA + acceptor
-
Homo sapiens but-2-enoyl-CoA + reduced acceptor
-
?
1.3.8.1 butanoyl-CoA + FAD
-
Homo sapiens but-2-enoyl-CoA + FADH2
-
?
1.3.8.1 hexanoyl-CoA + acceptor
-
Homo sapiens hex-2-enoyl-CoA + reduced acceptor
-
?
1.3.8.1 hexanoyl-CoA + FAD
-
Homo sapiens hex-2-enoyl-CoA + FADH2
-
?
1.3.8.1 pentanoyl-CoA + acceptor
-
Homo sapiens pent-2-enoyl-CoA + reduced acceptor
-
?
1.3.8.1 pentanoyl-CoA + FAD
-
Homo sapiens pent-2-enoyl-CoA + FADH2
-
?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.8.1 37
-
assay at Homo sapiens

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.3.8.1 26 41 activities of SCAD constructs are entirely lower at 26°C incubation temperature and slightly higher at 41°C incubation temperature than those at 37°C incubation temperature Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.8.1 7
-
assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.8.1 FAD
-
Homo sapiens

General Information

EC Number General Information Comment Organism
1.3.8.1 metabolism mutations in the gene encodine acyl-CoA dehydrogenase, ACAD, cause alterations in SCAD activity, overview Homo sapiens
1.3.8.1 physiological function SCAD is a mitochondrial enzyme involved in the beta-oxidation of fatty acids and mediates the metabolic transition from acyl-CoA with four or six carbon chains to 2-enoyl-CoA in the first step of the beta-oxidation spiral. Genetic defect of SCAD cause clinical symptoms such as progressive psychomotor retardation, muscle hypotonia, and myopathy Homo sapiens