Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-coA dehydrogenase from Megasphaera elsdenii

Megasphaera elsdenii reveals a short-chain acyl-CoA dehydrogenase (SCAD), which exhibits a molecular mechanism. The functioning is controlled by cloning and ordering the gene coding for SCAD. The suggested functioning needs an amino acid residue that is recognized by site-directed mutagenesis. Identification of the amino acid order of the 50 N-terminal residues of SCAD is required to clone the gene. Two groups of varying oligonucleotide primers are prepared by the order of the data, and a 120-bp specific probe from Megasphaera elsdenii DNA is produced by a polymerase chain reaction process.