RT Journal Article SR Electronic(1) A1 Zhang, Ying-Xin A1 Denoya, Claudio D. A1 Skinner, Deborah D. A1 Fedechko, Ronald W. A1 McArthur, Hamish A. I. A1 Morgenstern, Margaret R. A1 Davies, Richard A. A1 Lobo, Sandra A1 Reynolds, Kevin A. A1 Hutchinson, C. Richard YR 1999 T1 Genes encoding acyl-CoA dehydrogenase (AcdH) homologues from Streptomyces coelicolor and Streptomyces avermitilis provide insights into the metabolism of small branched-chain fatty acids and macrolide antibiotic productionThe GenBank accession numbers for the sequences described in this paper are AF142581 (Streptomyces coelicolor) and AF143210 (Streptomyces avermitilis). JF Microbiology, VO 145 IS 9 SP 2323 OP 2334 DO https://doi.org/10.1099/00221287-145-9-2323 PB Microbiology Society, SN 1465-2080, AB The cloning, using a PCR approach, of genes from both Streptomyces coelicolor and Streptomyces avermitilis encoding an acyl-CoA dehydrogenase (AcdH), putatively involved in the catabolism of branched-chain amino acids, is reported. The deduced amino acid sequences of both genes have a high similarity to prokaryotic and eukaryotic short-chain acyl-CoA dehydrogenases. When the S. coelicolor and S. avermitilis acyl-CoA dehydrogenase genes (acdH) were expressed in Escherichia coli, each of the AcdH flavoproteins was able to oxidize the branched-chain acyl-CoA derivatives isobutyryl-CoA, isovaleryl-CoA and cyclohexylcarbonyl-CoA, as well as the short straight-chain acyl-CoAs n-butyryl-CoA and n-valeryl-CoA in vitro. NMR spectral data confirmed that the oxidized product of isobutyryl-CoA is methacrylyl-CoA, which is the expected product at the acyl-CoA dehydrogenase step in the catabolism of valine in streptomycetes. Disruption of the S. avermitilis acdH produced a mutant unable to grow on solid minimal medium containing valine, isoleucine or leucine as sole carbon sources. Feeding studies with 13C triple-labelled isobutyrate revealed a significant decrease in the incorporation of label into the methylmalonyl-CoA-derived positions of avermectin in the acdH mutant. In contrast the mutation did not affect incorporation into the malonyl-CoA-derived positions of avermectin. These results are consistent with the acdH gene encoding an acyl-CoA dehydrogenase with a broad substrate specificity that has a role in the catabolism of branched-chain amino acids in S. coelicolor and S. avermitilis., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-145-9-2323