short-chain-acyl-CoA-dehydrogenase deficiency is an inborn error of mitochondrial fatty acid metabolism caused by rare mutations as well as common susceptibility variations in the SCAD gene
expression of acetyl-coenzyme A C-acetyltransferase, 3-hydroxybutyryl-CoA dehydrogenase, crotonase, phosphate butyryltransferase, and butyrate kinase and the butyryl-CoA dehydrogenase complex composed of the dehydrogenase and two electron-transferring flavoprotein subunits as a single plasmid-encoded operon in Escherichia coli to confer butyrate-forming capability
engineering of Clostridum sp. MT1962 by elimination of phosphotransacetylase and acetaldehyde dehydrogenase along with integration to chromosome synthetic thiolase, 3-hydroxybutyryl-CoA dehydrogenase, crotonase, butyryl-CoA dehydrogenase, butyraldehyde dehydrogenase, and NAD-dependent butanol dehydrogenase. Th resulting strain loses production of ethanol and acetate while initiated the production of 297 mM of n-butanol
engineering of Clostridum sp. MT1962 by elimination of phosphotransacetylase and acetaldehyde dehydrogenase along with integration to chromosome synthetic thiolase, 3-hydroxybutyryl-CoA dehydrogenase, crotonase, butyryl-CoA dehydrogenase, butyraldehyde dehydrogenase, and NAD-dependent butanol dehydrogenase. Th resulting strain loses production of ethanol and acetate while initiated the production of 297 mM of n-butanol
expression of acetyl-coenzyme A C-acetyltransferase, 3-hydroxybutyryl-CoA dehydrogenase, crotonase, phosphate butyryltransferase, and butyrate kinase and the butyryl-CoA dehydrogenase complex composed of the dehydrogenase and two electron-transferring flavoprotein subunits as a single plasmid-encoded operon in Escherichia coli to confer butyrate-forming capability
overall high degree of thermodynamic modulation of wild-type SCAD, substrate binding appears to make a larger contribution than does product to thermodynamic modulation, substrate redox activation leading to a large enzyme midpoint potential shift
type I strain has the same clustered genes with the same arrangement as type II strain, deduced amino acid sequences of these enzymes do not greatly differ between the two strains, and even between Butyrivibrio fibrisolvens and clostridia. Amino acid identity appears to be higher within the same type than between types I and II, clustered genes are cotranscribed, and constitutively transcribed without being affected significantly by culture conditions