{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kawai S"],"funding":["Japan Society for the Promotion of Science","New Energy and Industrial Technology Development Organization"],"pagination":["e202404790"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11973848"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(20)"],"pubmed_abstract":["Enzymes that catalyze regioselective and stereoselective hydroxylation of amino acids are useful tools for the synthesis of pharmaceuticals. AzpK is an unprecedented lysine 5-hydroxylase that is involved in alazopeptin biosynthesis, although its enzymatic activity has not been confirmed in vitro. Here, we identified two α-ketoglutarate/Fe<sup>2+</sup>-dependent dioxygenases in Actinosynnema mirum and Pseudomonas psychrotolerans (Am_AzpK2 and Pp_AzpK2, respectively) as lysine 5-hydroxylases, using genome mining based on the alazopeptin biosynthetic gene cluster. Interestingly, Am_AzpK2 and Pp_AzpK2 synthesized different isomers, (2S,5S)- and (2S,5R)-5-hydroxylysine, respectively. We also identified two AzpJ homologs as the dehydrogenases that specifically recognize the hydroxy groups of (2S"],"journal":["Chemistry (Weinheim an der Bergstrasse, Germany)"],"pubmed_title":["Identification of Two Distinct Stereoselective Lysine 5-Hydroxylases by Genome Mining Based on Alazopeptin Biosynthetic Enzymes."],"pmcid":["PMC11973848"],"funding_grant_id":["19H04645","22KJ1046","19H05685","22H05130"],"pubmed_authors":["Moriga K","Nirdnoy W","Ogawa J","Ohnishi Y","Hara R","Kawai S","Katsuyama Y"],"additional_accession":[]},"is_claimable":false,"name":"Identification of Two Distinct Stereoselective Lysine 5-Hydroxylases by Genome Mining Based on Alazopeptin Biosynthetic Enzymes.","description":"Enzymes that catalyze regioselective and stereoselective hydroxylation of amino acids are useful tools for the synthesis of pharmaceuticals. AzpK is an unprecedented lysine 5-hydroxylase that is involved in alazopeptin biosynthesis, although its enzymatic activity has not been confirmed in vitro. Here, we identified two α-ketoglutarate/Fe<sup>2+</sup>-dependent dioxygenases in Actinosynnema mirum and Pseudomonas psychrotolerans (Am_AzpK2 and Pp_AzpK2, respectively) as lysine 5-hydroxylases, using genome mining based on the alazopeptin biosynthetic gene cluster. Interestingly, Am_AzpK2 and Pp_AzpK2 synthesized different isomers, (2S,5S)- and (2S,5R)-5-hydroxylysine, respectively. We also identified two AzpJ homologs as the dehydrogenases that specifically recognize the hydroxy groups of (2S","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2025-07-14T03:02:48.936Z","creation":"2025-07-14T03:02:48.936Z"},"accession":"S-EPMC11973848","cross_references":{"pubmed":["39960436"],"doi":["10.1002/chem.202404790"]}}