Chemical Modification for the “Off‐/On” Regulation of Enzyme Activity

Abstract

Enzymes with excellent catalytic performance play important roles in living organisms. Advances in strategies for enzyme chemical modification have enabled powerful strategies for exploring and manipulating enzyme functions and activities. Based on the development of chemical enzyme modifications, incorporating external stimuli-responsive features-for example, responsivity to light, voltage, magnetic force, pH, temperature, redox activity, and small molecules-into a target enzyme to turn "on" and "off" its activity has attracted much attention. The ability to precisely control enzyme activity using different approaches will greatly expand the chemical biology toolbox for clarification and detection of signal transduction and in vivo enzyme function and significantly promote enzyme-based disease therapy. This review summarizes the methods available for chemical enzyme modification mainly for the off-/on control of enzyme activity and particularly highlights the recent progress regarding the applications of this strategy.

Relationship of Gene-Structure–Antioxidant Ability of Exopolysaccharides Derived from Lactic Acid Bacteria: A Review

“…74 Enzymatic modification can alter the activities and properties of enzymes and may be performed by nonspecific covalent modification, site-specific covalent modification, and noncovalent modification. 75 Dextran is a most common type of α-glucan, which can be altered by enzymatic modification using methods such as methylation analysis, enzymatic fingerprinting, and changes in the degree of branching and side chain length. The results of the analysis of glycosidic linkages and other structure characterizations using two-dimensional NMR spectroscopy indicate that the modified EPS retains the main structure of EPS and its molecular weight.…”

“…The substitution of certain amino acids in the active site like V288P, V291I, S396N, and A398S of these enzymes may subsequently alter the structure and antioxidant ability of EPS . Enzymatic modification can alter the activities and properties of enzymes and may be performed by nonspecific covalent modification, site-specific covalent modification, and noncovalent modification . Dextran is a most common type of α-glucan, which can be altered by enzymatic modification using methods such as methylation analysis, enzymatic fingerprinting, and changes in the degree of branching and side chain length.…”

Precise and Controlled Modification of Proteins using Multifunctional Chemical Constructs

“…The chemical modification of proteins in their native environment has provided detailed insights in their biological function and even enabled control over their biological role. [1][2][3][4][5][6][7][8] Alternatively, modification of isolated proteins has resulted in superior treatments, as is clear from the recent surge in the developments of antibody-drug conjugates (ADCs). [9] For both avenues, approaches have been developed to incorporate a unique chemically [10,11] and/or enzymatically [12][13][14][15][16] reactive moiety in the protein.…”

“…The chemical modification of proteins in their native environment has provided detailed insights in their biological function and even enabled control over their biological role [1–8] . Alternatively, modification of isolated proteins has resulted in superior treatments, as is clear from the recent surge in the developments of antibody‐drug conjugates (ADCs) [9] .…”

Phenylboronic acid‐functionalized glycogens as dynamic nano‐frameworks for conjugation and activation of carbonic anhydrase

“…[4][5][6][7][8] However, protein engineering, even the advanced method of directed evolution, is usually a time-consuming and laborious task, [9] while the covalent chemical modification on enzymes can possess a risk of altering the original structures of enzyme, which may even lead to the loss of catalytic activity. [10] Comparatively, additives present a straightforward strategy for enzyme activation, as long as beneficial enzyme interactions can be delicately designed. For example, poly(carboxybetaine) conjugation has been reported to improve the stability and binding affinity of the target protein.…”