{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Harwood SL"],"funding":["LEO Foundation","Novo Nordisk Fonden"],"pagination":["16732-16742"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7864068"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["295(49)"],"pubmed_abstract":["Proteins in the α-macroglobulin (αM) superfamily use thiol esters to form covalent conjugation products upon their proteolytic activation. αM protease inhibitors use theirs to conjugate proteases and preferentially react with primary amines (<i>e.g.</i> on lysine side chains), whereas those of αM complement components C3 and C4B have an increased hydroxyl reactivity that is conveyed by a conserved histidine residue and allows conjugation to cell surface glycans. Human α<sub>2</sub>-macroglobulin-like protein 1 (A2ML1) is a monomeric protease inhibitor but has the hydroxyl reactivity-conveying histidine residue. Here, we have investigated the role of hydroxyl reactivity in a protease inhibitor by comparing recombinant WT A2ML1 and the A2ML1 H1084N mutant in which this histidine is removed. "],"journal":["The Journal of biological chemistry"],"pubmed_title":["α<sub>2</sub>-Macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester."],"pmcid":["PMC7864068"],"funding_grant_id":["NNF18OC0032724","LF18039"],"pubmed_authors":["Nielsen NS","Harwood SL","Enghild JJ","Nielsen PK","Thogersen IB","Jensen KT"],"additional_accession":[]},"is_claimable":false,"name":"α<sub>2</sub>-Macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester.","description":"Proteins in the α-macroglobulin (αM) superfamily use thiol esters to form covalent conjugation products upon their proteolytic activation. αM protease inhibitors use theirs to conjugate proteases and preferentially react with primary amines (<i>e.g.</i> on lysine side chains), whereas those of αM complement components C3 and C4B have an increased hydroxyl reactivity that is conveyed by a conserved histidine residue and allows conjugation to cell surface glycans. Human α<sub>2</sub>-macroglobulin-like protein 1 (A2ML1) is a monomeric protease inhibitor but has the hydroxyl reactivity-conveying histidine residue. Here, we have investigated the role of hydroxyl reactivity in a protease inhibitor by comparing recombinant WT A2ML1 and the A2ML1 H1084N mutant in which this histidine is removed. ","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Dec","modification":"2026-05-01T16:28:01.299Z","creation":"2022-02-10T15:48:31.536Z"},"accession":"S-EPMC7864068","cross_references":{"pubmed":["32978260"],"doi":["10.1074/jbc.RA120.015694"]}}