{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["16(6)"],"submitter":["Jensen CN"],"funding":["Biotechnology and Biological Sciences Research Council"],"pubmed_abstract":["The FAD-dependent monooxygenase HbpA from Pseudomonas azelaica HBP1 catalyses the hydroxylation of 2-hydroxybiphenyl (2HBP) to 2,3-dihydroxybiphenyl (23DHBP). HbpA has been used extensively as a model for studying flavoprotein hydroxylases under process conditions, and has also been subjected to directed-evolution experiments that altered its catalytic properties. The structure of HbpA has been determined in its apo and FAD-complex forms to resolutions of 2.76 and 2.03 Å, respectively. Comparisons of the HbpA structure with those of homologues, in conjunction with a model of the reaction product in the active site, reveal His48 as the most likely acid/base residue to be involved in the hydroxylation mechanism. Mutation of His48 to Ala resulted in an inactive enzyme. The structures of HbpA "],"journal":["Chembiochem : a European journal of chemical biology"],"pagination":["968-76"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4515095"],"repository":["biostudies-literature"],"pubmed_title":["Structures of the Apo and FAD-bound forms of 2-hydroxybiphenyl 3-monooxygenase (HbpA) locate activity hotspots identified by using directed evolution."],"pmcid":["PMC4515095"],"pubmed_authors":["Turkenburg JP","Frank A","Mielke T","Hart S","Man H","Jensen CN","Farrugia JE","Grogan G"],"additional_accession":[]},"is_claimable":false,"name":"Structures of the Apo and FAD-bound forms of 2-hydroxybiphenyl 3-monooxygenase (HbpA) locate activity hotspots identified by using directed evolution.","description":"The FAD-dependent monooxygenase HbpA from Pseudomonas azelaica HBP1 catalyses the hydroxylation of 2-hydroxybiphenyl (2HBP) to 2,3-dihydroxybiphenyl (23DHBP). HbpA has been used extensively as a model for studying flavoprotein hydroxylases under process conditions, and has also been subjected to directed-evolution experiments that altered its catalytic properties. The structure of HbpA has been determined in its apo and FAD-complex forms to resolutions of 2.76 and 2.03 Å, respectively. Comparisons of the HbpA structure with those of homologues, in conjunction with a model of the reaction product in the active site, reveal His48 as the most likely acid/base residue to be involved in the hydroxylation mechanism. Mutation of His48 to Ala resulted in an inactive enzyme. The structures of HbpA ","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Apr","modification":"2025-04-04T09:12:39.47Z","creation":"2019-03-27T01:55:48Z"},"accession":"S-EPMC4515095","cross_references":{"pubmed":["25737306"],"doi":["10.1002/cbic.201402701"]}}