Enzyme active sites: Identification and prediction of function using computational chemistry. (June 2022)

• Record Type: Journal Article
• Authors: Barnsley, Kelly K.; Ondrechen, Mary Jo
• Is Part Of: Current opinion in structural biology. Volume 74(2022)
• Publication Date: 2022-06
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2022.102384
• Languages: English
• ISSNs: 0959-440X

Abstract

Abstract: Understanding the biochemically active amino acids in proteins is a key factor to improve the knowledge of how enzymes work, to predict the function of newly discovered protein structures of unknown function, and to establish design principles for enzyme engineering. Here, we explore recently reported computational chemistry-based methods for the prediction of active amino acids in protein 3D structures, including biochemically important distal residues, and their implications for functional genomics, for enzyme design, and for enhancing understanding of the function of enzymes. Highlights: Active amino acids are computationally predictable in protein structures. Distal residues are biochemically important in enzyme activity. Local arrays of active residues can be used to predict biochemical function. Interactions between residues are important to consider in protein design.