||The enzyme, characterized from the bacterium Streptomyces collinus, is involved in a pathway that transforms shikimate to cyclohexane-1-carbonyl-CoA by a series of dehydration and double-bond reduction steps. Most of the steps in this process occur with the carboxylic acid activated as a coenzyme A thioester. The enzyme catalyses three steps in this pathway, also acting on (3R,4R)-3,4-dihydroxycyclohexa-1,5-diene-1-carbonyl-CoA and (5S)-5-hydroxycyclohex-1-ene-1-carbonyl-CoA.
||Reynolds, K.A., Wang, P., Fox, K.M., Speedie, M.K., Lam, Y. and Floss, H.G. Purification and characterization of a novel enoyl coenzyme A reductase from Streptomyces collinus. J. Bacteriol. 174 (1992) 3850–3854. [PMID: 1597409]
||Wang, P., Denoya, C.D., Morgenstern, M.R., Skinner, D.D., Wallace, K.K., Digate, R., Patton, S., Banavali, N., Schuler, G., Speedie, M.K. and Reynolds, K.A. Cloning and characterization of the gene encoding 1-cyclohexenylcarbonyl coenzyme A reductase from Streptomyces collinus. J. Bacteriol. 178 (1996) 6873–6881. [PMID: 8955309]