Monomeric and dimeric forms of cholesterol esterase from Candida cylindracea. Primary structure, identity in peptide patterns, and additional microheterogeneity

Cholesterol esterase from Candida cylindracea was separated into two fractions, corresponding to a dimeric and a monomeric form. Fingerprint analysis after lysine cleavages shows identical patterns, suggesting lack of primary differences. Crystals obtained from the two proteins differ and suggest the possibility of an equilibrium between the two forms, influenced by the substrate cholesterol linoleate, which appears to stabilize the more active, dimeric form. All crystals have dimers as the asymmetric unit. The primary structure of the enzyme was determined at the peptide level and shows only one difference, Leu-350 instead of Ile, from a DNA-deduced amino acid sequence, and conservation of features typical for cholesterol esterases characterized.