Improvement of the Activity of a Fungal Versatile-Lipase Toward Triglycerides: An in silico Mechanistic Description.

ABSTRACT: Some enzymes that belong to the Candida rugosa-like lipase family (abH03. 01) combine the activities of lipases and sterol esterases. Thus, they can act on water-insoluble carboxylic esters releasing long-chain fatty acids but also on sterol esters, although with different activity and affinity. The differences in the catalytic properties among the proteins of this family are explained by small changes in the hydrophobicity of some regions. One of such versatile enzymes is the sterol esterase/lipase from Ophiostoma piceae (OPE) that acts very efficiently on the two types of substrates. Structurally, OPE is characterized by the presence of a lid formed by a α-helix and two 3₁₀-helices rich in hydrophobic amino acids. In this study, the ope gene was modified b

SUBMITTER: Paya-Tormo L 

PROVIDER: S-EPMC6449727 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature