{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bouvier JT"],"funding":["NIGMS NIH HHS"],"pagination":["614-6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3977579"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(4)"],"pubmed_abstract":["Agrobacterium tumefaciens strain C58 can utilize d-galacturonate as a sole source of carbon via a pathway in which the first step is oxidation of d-galacturonate to D-galactaro-1,5-lactone. We have identified a novel enzyme, D-galactarolactone isomerase (GLI), that catalyzes the isomerizaton of D-galactaro-1,5-lactone to D-galactaro-1,4-lactone. GLI, a member of the functionally diverse amidohydrolase superfamily, is a homologue of LigI that catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate in lignin degradation. The ability of GLI to catalyze lactone isomerization instead of hydrolysis can be explained by the absence of the general basic catalysis used by 2-pyrone-4,6-dicarboxylate lactonase."],"journal":["Biochemistry"],"pubmed_title":["Galactaro δ-lactone isomerase: lactone isomerization by a member of the amidohydrolase superfamily."],"pmcid":["PMC3977579"],"funding_grant_id":["U54GM093342","P01GM071790"],"pubmed_authors":["Almo SC","Gerlt JA","Vetting M","Bouvier JT","Groninger-Poe FP"],"additional_accession":[]},"is_claimable":false,"name":"Galactaro δ-lactone isomerase: lactone isomerization by a member of the amidohydrolase superfamily.","description":"Agrobacterium tumefaciens strain C58 can utilize d-galacturonate as a sole source of carbon via a pathway in which the first step is oxidation of d-galacturonate to D-galactaro-1,5-lactone. We have identified a novel enzyme, D-galactarolactone isomerase (GLI), that catalyzes the isomerizaton of D-galactaro-1,5-lactone to D-galactaro-1,4-lactone. GLI, a member of the functionally diverse amidohydrolase superfamily, is a homologue of LigI that catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate in lignin degradation. The ability of GLI to catalyze lactone isomerization instead of hydrolysis can be explained by the absence of the general basic catalysis used by 2-pyrone-4,6-dicarboxylate lactonase.","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Feb","modification":"2024-11-09T18:10:05.854Z","creation":"2019-03-27T01:24:31Z"},"accession":"S-EPMC3977579","cross_references":{"pubmed":["24450804"],"doi":["10.1021/bi5000492"]}}