{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Orellana MS"],"funding":["University of Concepción","University of Concepción, Chile"],"pagination":["6438"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9224512"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(12)"],"pubmed_abstract":["Arginase catalyzes the hydrolysis of L-arginine into L-ornithine and urea. This enzyme has several analogies with agmatinase, which catalyzes the hydrolysis of agmatine into putrescine and urea. However, this contrasts with the highlighted specificity that each one presents for their respective substrate. A comparison of available crystal structures for arginases reveals an important difference in the extension of two loops located in the entrance of the active site. The first, denominated <i>loop A</i> (I129-L140) contains the residues that interact with the alpha carboxyl group or arginine of arginase, and the <i>loop B</i> (D181-P184) contains the residues that interact with the alpha amino group of arginine. In this work, to determine the importance of these loops in the specificity of"],"journal":["International journal of molecular sciences"],"pubmed_title":["New Insights into the Determinants of Specificity in Human Type I Arginase: Generation of a Mutant That Is Only Active with Agmatine as Substrate."],"pmcid":["PMC9224512"],"funding_grant_id":["217.037.022-1","VRID-Enlace 217.037.022-1"],"pubmed_authors":["Figueroa M","Garcia-Robles MA","Carvajal N","Gatica M","Uribe E","Orellana MS","Martinez-Oyanedel J","Jana GA","Medina FE","Tarifeno-Saldivia E"],"additional_accession":[]},"is_claimable":false,"name":"New Insights into the Determinants of Specificity in Human Type I Arginase: Generation of a Mutant That Is Only Active with Agmatine as Substrate.","description":"Arginase catalyzes the hydrolysis of L-arginine into L-ornithine and urea. This enzyme has several analogies with agmatinase, which catalyzes the hydrolysis of agmatine into putrescine and urea. However, this contrasts with the highlighted specificity that each one presents for their respective substrate. A comparison of available crystal structures for arginases reveals an important difference in the extension of two loops located in the entrance of the active site. The first, denominated <i>loop A</i> (I129-L140) contains the residues that interact with the alpha carboxyl group or arginine of arginase, and the <i>loop B</i> (D181-P184) contains the residues that interact with the alpha amino group of arginine. In this work, to determine the importance of these loops in the specificity of","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2026-04-08T11:09:44.024Z","creation":"2024-11-06T10:28:41.047Z"},"accession":"S-EPMC9224512","cross_references":{"pubmed":["35742891"],"doi":["10.3390/ijms23126438"]}}