An iron (II) dependent oxygenase performs the last missing step of plant lysine catabolism.

Autor: Thompson MG; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Plant and Microbial Biology, University of California-Berkeley, Berkeley, CA, USA., Blake-Hedges JM; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Chemistry, University of California-Berkeley, Berkeley, CA, USA., Pereira JH; Joint BioEnergy Institute, Emeryville, CA, USA.; Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA, USA., Hangasky JA; Department of Chemistry, University of California-Berkeley, Berkeley, CA, USA., Belcher MS; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Plant and Microbial Biology, University of California-Berkeley, Berkeley, CA, USA., Moore WM; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Plant and Microbial Biology, University of California-Berkeley, Berkeley, CA, USA., Barajas JF; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Energy Agile BioFoundry, Emeryville, CA, USA., Cruz-Morales P; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA., Washington LJ; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Plant and Microbial Biology, University of California-Berkeley, Berkeley, CA, USA., Haushalter RW; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA., Eiben CB; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Bioengineering, University of California-Berkeley, Berkeley, CA, 94720, USA., Liu Y; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA., Skyrud W; Department of Chemistry, University of California-Berkeley, Berkeley, CA, USA., Benites VT; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA., Barnum TP; Department of Plant and Microbial Biology, University of California-Berkeley, Berkeley, CA, USA., Baidoo EEK; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA., Scheller HV; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Plant and Microbial Biology, University of California-Berkeley, Berkeley, CA, USA., Marletta MA; Department of Chemistry, University of California-Berkeley, Berkeley, CA, USA.; Department of Molecular and Cellular Biology, University of California-Berkeley, Berkeley, CA, USA., Shih PM; Joint BioEnergy Institute, Emeryville, CA, USA.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Plant Biology, University of California-Davis, Davis, CA, USA.; Genome Center, University of California-Davis, Davis, CA, USA.; Environmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA., Adams PD; Joint BioEnergy Institute, Emeryville, CA, USA.; Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Bioengineering, University of California-Berkeley, Berkeley, CA, 94720, USA., Keasling JD; Joint BioEnergy Institute, Emeryville, CA, USA. jdkeasling@lbl.gov.; Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA. jdkeasling@lbl.gov.; Department of Bioengineering, University of California-Berkeley, Berkeley, CA, 94720, USA. jdkeasling@lbl.gov.; Department of Chemical and Biomolecular Engineering, University of California-Berkeley, Berkeley, CA, USA. jdkeasling@lbl.gov.; The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Lyngby, Denmark. jdkeasling@lbl.gov.; Center for Synthetic Biochemistry, Shenzhen Institutes for Advanced Technologies, Shenzhen, China. jdkeasling@lbl.gov.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2020 Jun 10; Vol. 11 (1), pp. 2931. Date of Electronic Publication: 2020 Jun 10.
DOI: 10.1038/s41467-020-16815-3
Abstrakt: Despite intensive study, plant lysine catabolism beyond the 2-oxoadipate (2OA) intermediate remains unvalidated. Recently we described a missing step in the D-lysine catabolism of Pseudomonas putida in which 2OA is converted to D-2-hydroxyglutarate (2HG) via hydroxyglutarate synthase (HglS), a DUF1338 family protein. Here we solve the structure of HglS to 1.1 Å resolution in substrate-free form and in complex with 2OA. We propose a successive decarboxylation and intramolecular hydroxylation mechanism forming 2HG in a Fe(II)- and O 2 -dependent manner. Specificity is mediated by a single arginine, highly conserved across most DUF1338 proteins. An Arabidopsis thaliana HglS homolog coexpresses with known lysine catabolism enzymes, and mutants show phenotypes consistent with disrupted lysine catabolism. Structural and biochemical analysis of Oryza sativa homolog FLO7 reveals identical activity to HglS despite low sequence identity. Our results suggest DUF1338-containing enzymes catalyze the same biochemical reaction, exerting the same physiological function across bacteria and eukaryotes.
Databáze: MEDLINE