On the enzymatic activity of albumin

Abstract

Albumin molecule, unlike molecules of many other plasma proteins, is not covered with carbohydrate shell. It plays a crucial role in maintaining of colloid osmotic pressure of the blood, and is able to bind and transport various endogenous and exogenous molecules. The enzymatic activity of albumin, the existence and the role of which most researchers are still skeptical to accept, is of the main interest to us. In this review, a history of the issue is traced, with particular attention to the esterase activity of albumin. The kinetic and thermodynamic characteristics of the interaction of albumin with some substrates are adduced, and possibility of albumin being attributed to certain groups of Enzyme Nomenclature is considered.

Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates

“…For both HSA and BSA, the site Tyr411(410) is the primary site of phosphorylation: additional conditions (binding of modulators at other sites) are not required for the productive binding of an OPs molecules and, according to the data of MD simulation, the mechanism of the phosphorylation reaction is the same for both proteins. These data agree with the data of our previous studies [ 84 , 85 , 86 , 87 ] and with in vitro experiments [ 88 , 26 ]. Therefore, for irreversible binding of the OPs without additional modulators, we can expect similar results for HSA and BSA.…”

Serum Albumin

“…Albumin is not only the passive but also the active participant of the pharmacokinetic and toxicokinetic processes. Numerous experiments showed the esterase or pseudoesterase activity of albumin against α-naphtylacetate and p-nitrophenylacetate (NPA), fatty acid esters, aspirin, ketoprofene glucuronide, cyclophosphamide, nicotinic acid esters, octanoyl ghrelin, nitroacetanilide, nitrofluoroacetanilide and organophosphorus pesticides [17][18][19]. Acetylation is a typical example of the pseudoesterase activity of albumin when the consumption of the substrate is due to the formation of covalent bonds with the participation of many amino acid residues of the albumin molecule.…”

Organosulfur Compounds as Nutraceuticals

“…Disulfides show a distinct preference for dihedral angles approaching 90°. The binding and enzymatic properties of albumin were recently revised (Goncharov et al, 2015c); its Cys34 plays a significant role in the redox status of blood plasma. Because divalent sulfur is polarizable, the S-S bond is susceptible to scission by polar reagents, both EPs, and especially nucleophiles.…”

“…Albumin is a major plasma protein and contributes greatly to the plasma protein-SH pool. Thus, the search for new properties of albumin under the influence of OSC is also important, both with in silico and kinetic studies Goncharov et al, 2015c). Thus, the search for new properties of albumin under the influence of OSC is also important, both with in silico and kinetic studies Goncharov et al, 2015c).…”