{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10"],"submitter":["Reinbothe S"],"pubmed_abstract":["Higher plants contain a small, 5-member family of Rieske non-heme oxygenases that comprise the inner plastid envelope protein TIC55, phaeophorbide <i>a</i> oxygenasee (PAO), chlorophyllide <i>a</i> oxygenase (CAO), choline monooxygenase, and a 52 kDa protein (PTC52) associated with the precursor NADPH:protochlorophyllide (Pchlide) oxidoreductase A (pPORA) A translocon (PTC). Some of these chloroplast proteins have documented roles in chlorophyll biosynthesis (CAO) and degradation (PAO and TIC55), whereas the function of PTC52 remains unresolved. Biochemical evidence provided here identifies PTC52 as Pchlide <i>a</i> oxygenase of the inner plastid envelope linking Pchlide <i>b</i> synthesis to pPORA import. Protochlorophyllide <i>b</i> is the preferred substrate of PORA and its lack no long"],"journal":["Frontiers in plant science"],"pagination":["593"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6530659"],"repository":["biostudies-literature"],"pubmed_title":["A Protochlorophyllide (Pchlide) <i>a</i> Oxygenase for Plant Viability."],"pmcid":["PMC6530659"],"pubmed_authors":["Yuan S","Gray J","Reinbothe S","Reinbothe C","Bartsch S","Rossig C","Davis MY"],"additional_accession":[]},"is_claimable":false,"name":"A Protochlorophyllide (Pchlide) <i>a</i> Oxygenase for Plant Viability.","description":"Higher plants contain a small, 5-member family of Rieske non-heme oxygenases that comprise the inner plastid envelope protein TIC55, phaeophorbide <i>a</i> oxygenasee (PAO), chlorophyllide <i>a</i> oxygenase (CAO), choline monooxygenase, and a 52 kDa protein (PTC52) associated with the precursor NADPH:protochlorophyllide (Pchlide) oxidoreductase A (pPORA) A translocon (PTC). Some of these chloroplast proteins have documented roles in chlorophyll biosynthesis (CAO) and degradation (PAO and TIC55), whereas the function of PTC52 remains unresolved. Biochemical evidence provided here identifies PTC52 as Pchlide <i>a</i> oxygenase of the inner plastid envelope linking Pchlide <i>b</i> synthesis to pPORA import. Protochlorophyllide <i>b</i> is the preferred substrate of PORA and its lack no long","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019","modification":"2026-05-07T01:58:24.564Z","creation":"2019-07-01T13:54:19Z"},"accession":"S-EPMC6530659","cross_references":{"pubmed":["31156665"],"doi":["10.3389/fpls.2019.00593"]}}