Critical Enzyme Reactions in Aromatic Catabolism for Microbial Lignin Conversion

Erickson, Erika; Bleem, Alissa; Kuatsjah, Eugene; Werner, Allison Z.; DuBois, Jennifer L.; McGeehan, John E.; Eltis, Lindsay D.; Beckham, Gregg T.

doi:10.1038/s41929-022-00747-w

Title: Critical Enzyme Reactions in Aromatic Catabolism for Microbial Lignin Conversion

Journal Article · 25 February 2022 · Nature Catalysis

DOI:https://doi.org/10.1038/s41929-022-00747-w· OSTI ID:1855381

; Bleem, Alissa; Kuatsjah, Eugene;

; DuBois, Jennifer L.; McGeehan, John E.; Eltis, Lindsay D.;

The application of microbes to valorize aromatic compounds derived from the abundant plant biopolymer lignin is a rapidly developing area of research that may ultimately enable viable conversion of this recalcitrant and heterogeneous resource to valuable bio-based chemical products. Starting from the three canonical lignin building blocks, which differ in the extent of aromatic ring methoxylation, several common classes of enzymatic reaction occur in the upper pathways of aromatic catabolism to prepare aromatic compounds for assimilation into central carbon metabolism, including aromatic O-demethylation, hydroxylation and decarboxylation. These critical enzymatic steps can often be rate-limiting for efficient biological funnelling of aromatic compounds. Here we review the known enzymatic mechanisms for these reactions that are relevant for aerobic aromatic catabolism of lignin-related monomers, highlighting opportunities at the intersection of biochemistry, enzyme engineering and metabolic engineering for applications in the expanding field of microbial lignin valorization.

Cite

Export

Save

Research Organization:: National Renewable Energy Laboratory (NREL), Golden, CO (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Energy Efficiency and Renewable Energy (EERE), Sustainable Transportation Office. Bioenergy Technologies Office (BETO)

DOE Contract Number:: AC36-08GO28308

OSTI ID:: 1855381

Report Number(s):: NREL/JA-2A00-80238; MainId:42441; UUID:6dc24f5d-e5e2-4a21-8867-0f22f4531aba; MainAdminID:64041

Journal Information:: Nature Catalysis, Vol. 5

Country of Publication:: United States

Language:: English

References (155)

Lignin Biosynthesis Boerjan, Wout; Ralph, John; Baucher, Marie Annual Review of Plant Biology, Vol. 54, Issue 1, p. 519-546 https://doi.org/10.1146/annurev.arplant.54.031902.134938	journal	June 2003
Lignin Monomers from beyond the Canonical Monolignol Biosynthetic Pathway: Another Brick in the Wall del Río, José C.; Rencoret, Jorge; Gutiérrez, Ana ACS Sustainable Chemistry & Engineering, Vol. 8, Issue 13 https://doi.org/10.1021/acssuschemeng.0c01109	journal	March 2020
Hydroxycinnamates in lignification Ralph, John Phytochemistry Reviews, Vol. 9, Issue 1, p. 65-83 https://doi.org/10.1007/s11101-009-9141-9	journal	August 2009
Process Design and Economics for the Conversion of Lignocellulosic Biomass to Hydrocarbons: Dilute-Acid and Enzymatic Deconstruction of Biomass to Sugars and Biological Conversion of Sugars to Hydrocarbons Davis, R.; Tao, L.; Tan, E. C. D. https://doi.org/10.2172/1107470 NREL/TP-5100-60223	report	October 2013
Life cycle assessment of adipic acid production from lignin Corona, Andrea; Biddy, Mary J.; Vardon, Derek R. Green Chemistry, Vol. 20, Issue 16 https://doi.org/10.1039/C8GC00868J	journal	January 2018
The Catalytic Valorization of Lignin for the Production of Renewable Chemicals Zakzeski, Joseph; Bruijnincx, Pieter C. A.; Jongerius, Anna L. Chemical Reviews, Vol. 110, Issue 6, p. 3552-3599 https://doi.org/10.1021/cr900354u	journal	June 2010
Lignin Valorization: Improving Lignin Processing in the Biorefinery Ragauskas, A. J.; Beckham, G. T.; Biddy, M. J. Science, Vol. 344, Issue 6185, p. 1246843-1246843 https://doi.org/10.1126/science.1246843	journal	May 2014
Paving the Way for Lignin Valorisation: Recent Advances in Bioengineering, Biorefining and Catalysis Rinaldi, Roberto; Jastrzebski, Robin; Clough, Matthew T. Angewandte Chemie International Edition, Vol. 55, Issue 29 https://doi.org/10.1002/anie.201510351	journal	June 2016
Chemicals from lignin: an interplay of lignocellulose fractionation, depolymerisation, and upgrading Schutyser, W.; Renders, T.; Van den Bosch, S. Chemical Society Reviews, Vol. 47, Issue 3 https://doi.org/10.1039/C7CS00566K	journal	January 2018
Bright Side of Lignin Depolymerization: Toward New Platform Chemicals Sun, Zhuohua; Fridrich, Bálint; de Santi, Alessandra Chemical Reviews, Vol. 118, Issue 2 https://doi.org/10.1021/acs.chemrev.7b00588	journal	January 2018
Lignin valorization through integrated biological funneling and chemical catalysis Linger, J. G.; Vardon, D. R.; Guarnieri, M. T. Proceedings of the National Academy of Sciences, Vol. 111, Issue 33, p. 12013-12018 https://doi.org/10.1073/pnas.1410657111	journal	August 2014
Enzymatic conversion of lignin into renewable chemicals Bugg, Timothy DH; Rahmanpour, Rahman Current Opinion in Chemical Biology, Vol. 29 https://doi.org/10.1016/j.cbpa.2015.06.009	journal	December 2015
Opportunities and challenges in biological lignin valorization Beckham, Gregg T.; Johnson, Christopher W.; Karp, Eric M. Current Opinion in Biotechnology, Vol. 42 https://doi.org/10.1016/j.copbio.2016.02.030	journal	December 2016
Biological valorization of low molecular weight lignin Abdelaziz, Omar Y.; Brink, Daniel P.; Prothmann, Jens Biotechnology Advances, Vol. 34, Issue 8 https://doi.org/10.1016/j.biotechadv.2016.10.001	journal	December 2016
Bacterial catabolism of lignin-derived aromatics: New findings in a recent decade: Update on bacterial lignin catabolism: Bacterial catabolism of lignin-derived aromatics Kamimura, Naofumi; Takahashi, Kenji; Mori, Kosuke Environmental Microbiology Reports, Vol. 9, Issue 6 https://doi.org/10.1111/1758-2229.12597	journal	November 2017
Identifying and creating pathways to improve biological lignin valorization Liu, Zhi-Hua; Le, Rosemary K.; Kosa, Matyas Renewable and Sustainable Energy Reviews, Vol. 105 https://doi.org/10.1016/j.rser.2019.02.009	journal	May 2019
A field of dreams: Lignin valorization into chemicals, materials, fuels, and health-care products Becker, Judith; Wittmann, Christoph Biotechnology Advances, Vol. 37, Issue 6 https://doi.org/10.1016/j.biotechadv.2019.02.016	journal	November 2019
Adipic acid production from lignin Vardon, Derek R.; Franden, Mary Ann; Johnson, Christopher W. Energy & Environmental Science, Vol. 8, Issue 2 https://doi.org/10.1039/C4EE03230F	journal	January 2015
Microbial degradation of aromatic compounds — from one strategy to four Fuchs, Georg; Boll, Matthias; Heider, Johann Nature Reviews Microbiology, Vol. 9, Issue 11, p. 803-816 https://doi.org/10.1038/nrmicro2652	journal	October 2011
Dioxygenase enzymes: catalytic mechanisms and chemical models Bugg, Timothy D. H. Tetrahedron, Vol. 59, Issue 36 https://doi.org/10.1016/S0040-4020(03)00944-X	journal	September 2003
The Ins and Outs of Ring-Cleaving Dioxygenases Vaillancourt, Frédéric H.; Bolin, Jeffrey T.; Eltis, Lindsay D. Critical Reviews in Biochemistry and Molecular Biology, Vol. 41, Issue 4 https://doi.org/10.1080/10409230600817422	journal	January 2006
Biocatalytic conversion of lignin to aromatic dicarboxylic acids in Rhodococcus jostii RHA1 by re-routing aromatic degradation pathways Mycroft, Zoe; Gomis, Maria; Mines, Paul Green Chemistry, Vol. 17, Issue 11 https://doi.org/10.1039/C5GC01347J	journal	January 2015
Metabolic engineering of Corynebacterium glutamicum for the production of cis, cis-muconic acid from lignin Becker, Judith; Kuhl, Martin; Kohlstedt, Michael Microbial Cell Factories, Vol. 17, Issue 1 https://doi.org/10.1186/s12934-018-0963-2	journal	July 2018
Discovery of novel enzyme genes involved in the conversion of an arylglycerol-β-aryl ether metabolite and their use in generating a metabolic pathway for lignin valorization Higuchi, Yudai; Kato, Ryo; Tsubota, Koichiro Metabolic Engineering, Vol. 55 https://doi.org/10.1016/j.ymben.2019.08.002	journal	September 2019
Innovative Chemicals and Materials from Bacterial Aromatic Catabolic Pathways Johnson, Christopher W.; Salvachúa, Davinia; Rorrer, Nicholas A. Joule, Vol. 3, Issue 6 https://doi.org/10.1016/j.joule.2019.05.011	journal	June 2019
Discovery of potential pathways for biological conversion of poplar wood into lipids by co-fermentation of Rhodococci strains Li, Xiaolu; He, Yucai; Zhang, Libing Biotechnology for Biofuels, Vol. 12, Issue 1 https://doi.org/10.1186/s13068-019-1395-x	journal	March 2019
Funneling aromatic products of chemically depolymerized lignin into 2-pyrone-4-6-dicarboxylic acid with Novosphingobium aromaticivorans Perez, Jose M.; Kontur, Wayne S.; Alherech, Manar Green Chemistry, Vol. 21, Issue 6 https://doi.org/10.1039/C8GC03504K	journal	January 2019
Development of the production of 2-pyrone-4,6-dicarboxylic acid from lignin extracts, which are industrially formed as by-products, as raw materials Suzuki, Yuzo; Okamura-Abe, Yuriko; Nakamura, Masaya Journal of Bioscience and Bioengineering, Vol. 130, Issue 1 https://doi.org/10.1016/j.jbiosc.2020.02.002	journal	July 2020
Enhancement of protocatechuate decarboxylase activity for the effective production of muconate from lignin-related aromatic compounds Sonoki, Tomonori; Morooka, Miyuki; Sakamoto, Kimitoshi Journal of Biotechnology, Vol. 192 https://doi.org/10.1016/j.jbiotec.2014.10.027	journal	December 2014
Enhancing muconic acid production from glucose and lignin-derived aromatic compounds via increased protocatechuate decarboxylase activity Johnson, Christopher W.; Salvachúa, Davinia; Khanna, Payal Metabolic Engineering Communications, Vol. 3 https://doi.org/10.1016/j.meteno.2016.04.002	journal	December 2016
Bioprocess development for muconic acid production from aromatic compounds and lignin Salvachúa, Davinia; Johnson, Christopher W.; Singer, Christine A. Green Chemistry, Vol. 20, Issue 21 https://doi.org/10.1039/C8GC02519C	journal	January 2018
Versatility of biological non-heme Fe(II) centers in oxygen activation reactions Kovaleva, Elena G.; Lipscomb, John D. Nature Chemical Biology, Vol. 4, Issue 3 https://doi.org/10.1038/nchembio.71	journal	February 2008
Oxidative dealkylation DNA repair mediated by the mononuclear non-heme iron AlkB proteins Mishina, Yukiko; He, Chuan Journal of Inorganic Biochemistry, Vol. 100, Issue 4 https://doi.org/10.1016/j.jinorgbio.2005.12.018	journal	April 2006
The roles of DNA, RNA and histone methylation in ageing and cancer Michalak, Ewa M.; Burr, Marian L.; Bannister, Andrew J. Nature Reviews Molecular Cell Biology, Vol. 20, Issue 10 https://doi.org/10.1038/s41580-019-0143-1	journal	July 2019
Rieske business: Structure–function of Rieske non-heme oxygenases Ferraro, Daniel J.; Gakhar, Lokesh; Ramaswamy, S. Biochemical and Biophysical Research Communications, Vol. 338, Issue 1 https://doi.org/10.1016/j.bbrc.2005.08.222	journal	December 2005
A new classification system for bacterial Rieske non-heme iron aromatic ring-hydroxylating oxygenases Kweon, Ohgew; Kim, Seong-Jae; Baek, Songjoon BMC Biochemistry, Vol. 9, Issue 1 https://doi.org/10.1186/1471-2091-9-11	journal	January 2008
Cytochrome P450 systems—biological variations of electron transport chains Hannemann, Frank; Bichet, Andreas; Ewen, Kerstin M. Biochimica et Biophysica Acta (BBA) - General Subjects, Vol. 1770, Issue 3 https://doi.org/10.1016/j.bbagen.2006.07.017	journal	March 2007
A Novel Tetrahydrofolate-Dependent O-Demethylase Gene Is Essential for Growth of Sphingomonas paucimobilis SYK-6 with Syringate Masai, E.; Sasaki, M.; Minakawa, Y. Journal of Bacteriology, Vol. 186, Issue 9 https://doi.org/10.1128/JB.186.9.2757-2765.2004	journal	April 2004
A Tetrahydrofolate-Dependent O-Demethylase, LigM, Is Crucial for Catabolism of Vanillate and Syringate in Sphingomonas paucimobilis SYK-6 Abe, T.; Masai, E.; Miyauchi, K. Journal of Bacteriology, Vol. 187, Issue 6, p. 2030-2037 https://doi.org/10.1128/JB.187.6.2030-2037.2005	journal	March 2005
Cytochrome P450: taming a wild type enzyme Jung, Sang Taek; Lauchli, Ryan; Arnold, Frances H. Current Opinion in Biotechnology, Vol. 22, Issue 6 https://doi.org/10.1016/j.copbio.2011.02.008	journal	December 2011
Pseudomonas putida as a functional chassis for industrial biocatalysis: From native biochemistry to trans-metabolism Nikel, Pablo I.; de Lorenzo, Víctor Metabolic Engineering, Vol. 50 https://doi.org/10.1016/j.ymben.2018.05.005	journal	November 2018
Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase. Brunel, F.; Davison, J. Journal of Bacteriology, Vol. 170, Issue 10 https://doi.org/10.1128/jb.170.10.4924-4930.1988	journal	October 1988
Vanillate O-demethylase from Pseudomonas species Buswell, John A.; Ribbons, Douglas W. Methods in Enzymology https://doi.org/10.1016/0076-6879(88)61032-9	book	January 1988
Metabolism of syringyl lignin-derived compounds in Pseudomonas putida enables convergent production of 2-pyrone-4,6-dicarboxylic acid Notonier, Sandra; Werner, Allison Z.; Kuatsjah, Eugene Metabolic Engineering, Vol. 65 https://doi.org/10.1016/j.ymben.2021.02.005	journal	May 2021
Functional coupling between vanillate- O -demethylase and formaldehyde detoxification pathway Hibi, Makoto; Sonoki, Tomonori; Mori, Hideo FEMS Microbiology Letters, Vol. 253, Issue 2 https://doi.org/10.1016/j.femsle.2005.09.036	journal	December 2005
Exploring the Selective Demethylation of Aryl Methyl Ethers with a Pseudomonas Rieske Monooxygenase Lanfranchi, Elisa; Trajković, Miloš; Barta, Katalin ChemBioChem, Vol. 20, Issue 1 https://doi.org/10.1002/cbic.201800594	journal	December 2018
Cytochromes P450 and drug discovery Lamb, David C.; Waterman, Michael R.; Kelly, Steven L. Current Opinion in Biotechnology, Vol. 18, Issue 6 https://doi.org/10.1016/j.copbio.2007.09.010	journal	December 2007
Redox Partners: Function Modulators of Bacterial P450 Enzymes Li, Shengying; Du, Lei; Bernhardt, Rita Trends in Microbiology, Vol. 28, Issue 6 https://doi.org/10.1016/j.tim.2020.02.012	journal	June 2020
Self-Sufficient Class VII Cytochromes P450: From Full-Length Structure to Synthetic Biology Applications Correddu, Danilo; Di Nardo, Giovanna; Gilardi, Gianfranco Trends in Biotechnology, Vol. 39, Issue 11 https://doi.org/10.1016/j.tibtech.2021.01.011	journal	November 2021
Rate-Limiting Steps in Cytochrome P450 Catalysis Guengerich, F. P. Biological Chemistry, Vol. 383, Issue 10 https://doi.org/10.1515/BC.2002.175	journal	January 2002
Purification and characterization of cytochrome P450RR1 from Rhodococcus rhodochrous Eltis, Lindsay D.; Karlson, Ulrich; Timmis, Kenneth N. European Journal of Biochemistry, Vol. 213, Issue 1 https://doi.org/10.1111/j.1432-1033.1993.tb17750.x	journal	April 1993
Two independently regulated cytochromes P-450 in a Rhodococcus rhodochrous strain that degrades 2-ethoxyphenol and 4-methoxybenzoate. Karlson, U.; Dwyer, D. F.; Hooper, S. W. Journal of Bacteriology, Vol. 175, Issue 5 https://doi.org/10.1128/jb.175.5.1467-1474.1993	journal	March 1993
Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris Bell, Stephen G.; Hoskins, Nicola; Xu, Feng Biochemical and Biophysical Research Communications, Vol. 342, Issue 1 https://doi.org/10.1016/j.bbrc.2006.01.133	journal	March 2006
Crystal Structure of CYP199A2, a Para-Substituted Benzoic Acid Oxidizing Cytochrome P450 from Rhodopseudomonas palustris Bell, Stephen G.; Xu, Feng; Forward, Ian Journal of Molecular Biology, Vol. 383, Issue 3 https://doi.org/10.1016/j.jmb.2008.08.033	journal	November 2008
Accelerating pathway evolution by increasing the gene dosage of chromosomal segments Tumen-Velasquez, Melissa; Johnson, Christopher W.; Ahmed, Alaa Proceedings of the National Academy of Sciences, Vol. 115, Issue 27 https://doi.org/10.1073/pnas.1803745115	journal	June 2018
Enabling microbial syringol conversion through structure-guided protein engineering Machovina, Melodie M.; Mallinson, Sam J. B.; Knott, Brandon C. Proceedings of the National Academy of Sciences, Vol. 116, Issue 28 https://doi.org/10.1073/pnas.1820001116	journal	June 2019
Engineering a Cytochrome P450 for Demethylation of Lignin-Derived Aromatic Aldehydes Ellis, Emerald S.; Hinchen, Daniel J.; Bleem, Alissa JACS Au, Vol. 1, Issue 3 https://doi.org/10.1021/jacsau.0c00103	journal	February 2021
Characterization of alkylguaiacol-degrading cytochromes P450 for the biocatalytic valorization of lignin Fetherolf, Morgan M.; Levy-Booth, David J.; Navas, Laura E. Proceedings of the National Academy of Sciences, Vol. 117, Issue 41 https://doi.org/10.1073/pnas.1916349117	journal	September 2020
Cytochrome P450 diversity in the tree of life Nelson, David R. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol. 1866, Issue 1 https://doi.org/10.1016/j.bbapap.2017.05.003	journal	January 2018
Purification and characterization of 2-ethoxyphenol-induced cytochrome P450 from Corynebacterium sp. strain EP1 Kawahara, Naoko; Ikatsu, Hisayoshi; Kawata, Hiroshige Canadian Journal of Microbiology, Vol. 45, Issue 10 https://doi.org/10.1139/w99-082	journal	October 1999
Demethylation of Veratrole by Cytochrome P-450 in Streptomyces setonii Sutherland, John B. Applied and Environmental Microbiology, Vol. 52, Issue 1 https://doi.org/10.1128/aem.52.1.98-100.1986	journal	January 1986
Purification and properties of cytochrome P-450 from Moraxella sp. Sauret-Ignazi, Ginette; Dardas, Anastase; Pelmont, Jean Biochimie, Vol. 70, Issue 10 https://doi.org/10.1016/S0300-9084(88)80001-4	journal	October 1988
Identification of the two-component guaiacol demethylase system from Rhodococcus rhodochrous and expression in Pseudomonas putida EM42 for guaiacol assimilation García-Hidalgo, Javier; Ravi, Krithika; Kuré, Lise-Lotte AMB Express, Vol. 9, Issue 1 https://doi.org/10.1186/s13568-019-0759-8	journal	March 2019
Expression and characterization of the benzoic acid hydroxylase CYP199A25 from Arthrobacter sp. Klenk, Jan M.; Ertl, Julia; Rapp, Lea Molecular Catalysis, Vol. 484 https://doi.org/10.1016/j.mcat.2019.110739	journal	March 2020
Regioselective aromatic O -demethylation with an artificial P450BM3 peroxygenase system Jiang, Yihui; Wang, Chunlan; Ma, Nana Catalysis Science & Technology, Vol. 10, Issue 5 https://doi.org/10.1039/D0CY00241K	journal	January 2020
Promoting Lignin Valorization by Coping with Toxic C1 Byproducts Zhang, Zhihui; Wang, Yu; Zheng, Ping Trends in Biotechnology, Vol. 39, Issue 4 https://doi.org/10.1016/j.tibtech.2020.09.005	journal	April 2021
Sources of one-carbon units in the folate pathway of Escherichia coli. Dev, I. K.; Harvey, R. J. Journal of Biological Chemistry, Vol. 257, Issue 4 https://doi.org/10.1016/S0021-9258(19)68135-4	journal	February 1982
Tetrahydrofolate-dependent vanillate and syringateO-demethylation links tightly to one-carbon metabolic pathway associated with amino acid synthesis and DNA methylation in the lignin metabolism ofSphingomonas paucimobilis SYK-6 Sonoki, Tomonori; Otsuka, Yuichiro; Ikeda, Seiichiro Journal of Wood Science, Vol. 48, Issue 5 https://doi.org/10.1007/BF00770706	journal	October 2002
The crystal structure of a new O ‐demethylase from Sphingobium sp. strain SYK ‐6 Harada, Ayaka; Kamimura, Naofumi; Takeuchi, Koh The FEBS Journal, Vol. 284, Issue 12 https://doi.org/10.1111/febs.14085	journal	May 2017
Structure of aryl O -demethylase offers molecular insight into a catalytic tyrosine-dependent mechanism Kohler, Amanda C.; Mills, Matthew J. L.; Adams, Paul D. Proceedings of the National Academy of Sciences, Vol. 114, Issue 16 https://doi.org/10.1073/pnas.1619263114	journal	April 2017
Redundancy in Aromatic O -Demethylation and Ring-Opening Reactions in Novosphingobium aromaticivorans and Their Impact in the Metabolism of Plant-Derived Phenolics Perez, Jose M.; Kontur, Wayne S.; Gehl, Carson Applied and Environmental Microbiology, Vol. 87, Issue 8 https://doi.org/10.1128/AEM.02794-20	journal	March 2021
Isolation of O -demethylase, an ether-cleaving enzyme system of the homoacetogenic strain MC Kaufmann, Franz; Wohlfarth, Gert; Diekert, G. Archives of Microbiology, Vol. 168, Issue 2 https://doi.org/10.1007/s002030050479	journal	August 1997
Characterization of a Three-Component Vanillate O-Demethylase from Moorella thermoacetica Naidu, D.; Ragsdale, S. W. Journal of Bacteriology, Vol. 183, Issue 11 https://doi.org/10.1128/JB.183.11.3276-3281.2001	journal	June 2001
Characterization of an O-Demethylase of Desulfitobacterium hafniense DCB-2 Studenik, S.; Vogel, M.; Diekert, G. Journal of Bacteriology, Vol. 194, Issue 13, p. 3317-3326 https://doi.org/10.1128/JB.00146-12	journal	April 2012
Lignin structure and its engineering Ralph, John; Lapierre, Catherine; Boerjan, Wout Current Opinion in Biotechnology, Vol. 56 https://doi.org/10.1016/j.copbio.2019.02.019	journal	April 2019
Monooxygenation of aromatic compounds by flavin-dependent monooxygenases: Flavin-dependent Aromatic Hydroxylases Chenprakhon, Pirom; Wongnate, Thanyaporn; Chaiyen, Pimchai Protein Science, Vol. 28, Issue 1 https://doi.org/10.1002/pro.3525	journal	December 2018
Mechanism of Aromatic Amino Acid Hydroxylation ^† Fitzpatrick, Paul F. Biochemistry, Vol. 42, Issue 48 https://doi.org/10.1021/bi035656u	journal	December 2003
The versatility of the fungal cytochrome P450 monooxygenase system is instrumental in xenobiotic detoxification: Fungal P450 systems in xenobiotic detoxification Lah, Ljerka; Podobnik, Barbara; Novak, Metka Molecular Microbiology, Vol. 81, Issue 5 https://doi.org/10.1111/j.1365-2958.2011.07772.x	journal	August 2011
Multiple Roles of Component Proteins in Bacterial Multicomponent Monooxygenases: Phenol Hydroxylase and Toluene/ o -Xylene Monooxygenase from Pseudomonas sp. OX1 Tinberg, Christine E.; Song, Woon Ju; Izzo, Viviana Biochemistry, Vol. 50, Issue 11 https://doi.org/10.1021/bi200028z	journal	March 2011
NahW, a Novel, Inducible Salicylate Hydroxylase Involved in Mineralization of Naphthalene by Pseudomonas stutzeri AN10 Bosch, Rafael; Moore, Edward R. B.; García-Valdés, Elena Journal of Bacteriology, Vol. 181, Issue 8 https://doi.org/10.1128/JB.181.8.2315-2322.1999	journal	April 1999
Biphenyl Dioxygenases: Functional Versatilities and Directed Evolution Furukawa, Kensuke; Suenaga, Hikaru; Goto, Masatoshi Journal of Bacteriology, Vol. 186, Issue 16 https://doi.org/10.1128/JB.186.16.5189-5196.2004	journal	August 2004
Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases Neidle, E. L.; Hartnett, C.; Ornston, L. N. Journal of Bacteriology, Vol. 173, Issue 17 https://doi.org/10.1128/jb.173.17.5385-5395.1991	journal	September 1991
Structure and mechanism of para-hydroxybenzoate hydroxylase. Entsch, B.; van Berkel, W. J. The FASEB Journal, Vol. 9, Issue 7 https://doi.org/10.1096/fasebj.9.7.7737455	journal	April 1995
Switch of coenzyme specificity of p -hydroxybenzoate hydroxylase 1 1Edited by A. R. Fersht Eppink, Michel H. M.; Overkamp, Karin M.; Schreuder, Herman A. Journal of Molecular Biology, Vol. 292, Issue 1 https://doi.org/10.1006/jmbi.1999.3015	journal	September 1999
Genetic and biochemical characterization of a 4-hydroxybenzoate hydroxylase from Corynebacterium glutamicum Huang, Yan; Zhao, Ke-xin; Shen, Xi-Hui Applied Microbiology and Biotechnology, Vol. 78, Issue 1 https://doi.org/10.1007/s00253-007-1286-0	journal	December 2007
Uncovering the Protocatechuate 2,3-Cleavage Pathway Genes Kasai, Daisuke; Fujinami, Toshihiro; Abe, Tomokuni Journal of Bacteriology, Vol. 191, Issue 21 https://doi.org/10.1128/JB.00840-09	journal	November 2009
Flavin dependent monooxygenases Huijbers, Mieke M. E.; Montersino, Stefania; Westphal, Adrie H. Archives of Biochemistry and Biophysics, Vol. 544 https://doi.org/10.1016/j.abb.2013.12.005	journal	February 2014
The enigmatic reaction of flavins with oxygen Chaiyen, Pimchai; Fraaije, Marco W.; Mattevi, Andrea Trends in Biochemical Sciences, Vol. 37, Issue 9 https://doi.org/10.1016/j.tibs.2012.06.005	journal	September 2012
The FMN-dependent two-component monooxygenase systems Ellis, Holly R. Archives of Biochemistry and Biophysics, Vol. 497, Issue 1-2 https://doi.org/10.1016/j.abb.2010.02.007	journal	May 2010
The Reductase of p -Hydroxyphenylacetate 3-Hydroxylase from Acinetobacter baumannii Requires p -Hydroxyphenylacetate for Effective Catalysis ^† Sucharitakul, Jeerus; Chaiyen, Pimchai; Entsch, Barrie Biochemistry, Vol. 44, Issue 30 https://doi.org/10.1021/bi050615e	journal	August 2005
Control of catalysis in flavin-dependent monooxygenases Palfey, Bruce A.; McDonald, Claudia A. Archives of Biochemistry and Biophysics, Vol. 493, Issue 1 https://doi.org/10.1016/j.abb.2009.11.028	journal	January 2010
Phenol/cresol degradation by the thermophilic Bacillus thermoglucosidasius A7: cloning and sequence analysis of five genes involved in the pathway Duffner, Fiona M.; Kirchner, Ulrike; Bauer, Michael P. Gene, Vol. 256, Issue 1-2 https://doi.org/10.1016/S0378-1119(00)00352-8	journal	October 2000
Catabolism of Alkylphenols in Rhodococcus via a Meta-Cleavage Pathway Associated With Genomic Islands Levy-Booth, David J.; Fetherolf, Morgan M.; Stewart, Gordon R. Frontiers in Microbiology, Vol. 10 https://doi.org/10.3389/fmicb.2019.01862	journal	August 2019
Kinetic Mechanisms of the Oxygenase from a Two-component Enzyme, p-Hydroxyphenylacetate 3-Hydroxylase from Acinetobacter baumannii Sucharitakul, Jeerus; Chaiyen, Pimchai; Entsch, Barrie Journal of Biological Chemistry, Vol. 281, Issue 25 https://doi.org/10.1074/jbc.M512385200	journal	June 2006
Variation of the contents of biphenyl structures in lignins among wood species Hirayama, Haruka; Akiyama, Takuya; Tamai, Akari Holzforschung, Vol. 73, Issue 6 https://doi.org/10.1515/hf-2018-0196	journal	January 2019
Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl dioxygenase Kumamaru, Tetsuya; Suenaga, Hikaru; Mitsuoka, Mariko Nature Biotechnology, Vol. 16, Issue 7 https://doi.org/10.1038/nbt0798-663	journal	July 1998
Salicylate 5-Hydroxylase: Intermediates in Aromatic Hydroxylation by a Rieske Monooxygenase Rogers, Melanie S.; Lipscomb, John D. Biochemistry, Vol. 58, Issue 52 https://doi.org/10.1021/acs.biochem.9b00292	journal	May 2019
Purification and characterization of salicylate 5-hydroxylase, a three-component monooxygenase from Ralstonia sp. strain U2 Fang, Ti; Zhou, Ning-Yi Applied Microbiology and Biotechnology, Vol. 98, Issue 2 https://doi.org/10.1007/s00253-013-4914-x	journal	April 2013
Substrate Specificity of Naphthalene Dioxygenase: Effect of Specific Amino Acids at the Active Site of the Enzyme Parales, Rebecca E.; Lee, Kyoung; Resnick, Sol M. Journal of Bacteriology, Vol. 182, Issue 6 https://doi.org/10.1128/JB.182.6.1641-1649.2000	journal	March 2000
Engineering Rieske Non‐Heme Iron Oxygenases for the Asymmetric Dihydroxylation of Alkenes Gally, Christine; Nestl, Bettina M.; Hauer, Bernhard Angewandte Chemie International Edition, Vol. 54, Issue 44 https://doi.org/10.1002/anie.201506527	journal	September 2015
One enzyme, many reactions: structural basis for the various reactions catalyzed by naphthalene 1,2-dioxygenase Ferraro, Daniel J.; Okerlund, Adam; Brown, Eric IUCrJ, Vol. 4, Issue 5 https://doi.org/10.1107/S2052252517008223	journal	August 2017
Purification and Characterization of a Three-Component Salicylate 1-Hydroxylase from Sphingomonas sp. Strain CHY-1 Jouanneau, Yves; Micoud, Julien; Meyer, Christine Applied and Environmental Microbiology, Vol. 73, Issue 23 https://doi.org/10.1128/AEM.01519-07	journal	December 2007
Intracellular pathways for lignin catabolism in white-rot fungi del Cerro, Carlos; Erickson, Erika; Dong, Tao Proceedings of the National Academy of Sciences, Vol. 118, Issue 9 https://doi.org/10.1073/pnas.2017381118	journal	February 2021
Structural and Catalytic Diversity within the Amidohydrolase Superfamily ^† Seibert, Clara M.; Raushel, Frank M. Biochemistry, Vol. 44, Issue 17 https://doi.org/10.1021/bi047326v	journal	May 2005
Decarboxylation mechanisms in biological system Li, Tingfeng; Huo, Lu; Pulley, Christopher Bioorganic Chemistry, Vol. 43 https://doi.org/10.1016/j.bioorg.2012.03.001	journal	August 2012
Substrate Distortion and the Catalytic Reaction Mechanism of 5-Carboxyvanillate Decarboxylase Vladimirova, Anna; Patskovsky, Yury; Fedorov, Alexander A. Journal of the American Chemical Society, Vol. 138, Issue 3 https://doi.org/10.1021/jacs.5b08251	journal	January 2016
Mechanism and Structure of γ-Resorcylate Decarboxylase Sheng, Xiang; Patskovsky, Yury; Vladimirova, Anna Biochemistry, Vol. 57, Issue 22 https://doi.org/10.1021/acs.biochem.7b01213	journal	December 2017
A Combined Experimental-Theoretical Study of the LigW-Catalyzed Decarboxylation of 5-Carboxyvanillate in the Metabolic Pathway for Lignin Degradation Sheng, Xiang; Zhu, Wen; Huddleston, Jamison ACS Catalysis, Vol. 7, Issue 8 https://doi.org/10.1021/acscatal.7b01166	journal	June 2017
A Second 5-Carboxyvanillate Decarboxylase Gene, ligW2 , Is Important for Lignin-Related Biphenyl Catabolism in Sphingomonas paucimobilis SYK-6 Peng, Xue; Masai, Eiji; Kasai, Daisuke Applied and Environmental Microbiology, Vol. 71, Issue 9 https://doi.org/10.1128/AEM.71.9.5014-5021.2005	journal	September 2005
γ-Resorcylate Catabolic-Pathway Genes in the Soil Actinomycete Rhodococcus jostii RHA1 Kasai, Daisuke; Araki, Naoto; Motoi, Kota Applied and Environmental Microbiology, Vol. 81, Issue 21 https://doi.org/10.1128/AEM.02422-15	journal	November 2015
The Hydroxyquinol Degradation Pathway in Rhodococcus jostii RHA1 and Agrobacterium Species Is an Alternative Pathway for Degradation of Protocatechuic Acid and Lignin Fragments Spence, Edward M.; Scott, Heather T.; Dumond, Louison Applied and Environmental Microbiology, Vol. 86, Issue 19 https://doi.org/10.1128/AEM.01561-20	journal	September 2020
Agdc1p – a Gallic Acid Decarboxylase Involved in the Degradation of Tannic Acid in the Yeast Blastobotrys (Arxula) adeninivorans Meier, Anna K.; Worch, Sebastian; Böer, Erik Frontiers in Microbiology, Vol. 8 https://doi.org/10.3389/fmicb.2017.01777	journal	September 2017
An expanded enzyme toolbox for production of cis, cis-muconic acid and other shikimate pathway derivatives in Saccharomyces cerevisiae Brückner, Christine; Oreb, Mislav; Kunze, Gotthard FEMS Yeast Research, Vol. 18, Issue 2 https://doi.org/10.1093/femsyr/foy017	journal	February 2018
Crystal structures of non-oxidative decarboxylases reveal a new mechanism of action with a catalytic dyad and structural twists Zeug, Matthias; Markovic, Nebojsa; Iancu, Cristina V. Scientific Reports, Vol. 11, Issue 1 https://doi.org/10.1038/s41598-021-82660-z	journal	February 2021
UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis White, Mark D.; Payne, Karl A. P.; Fisher, Karl Nature, Vol. 522, Issue 7557 https://doi.org/10.1038/nature14559	journal	June 2015
Distribution of genes encoding the microbial non-oxidative reversible hydroxyarylic acid decarboxylases/phenol carboxylases☆ Lupa, B.; Lyon, D.; Gibbs, M. Genomics, Vol. 86, Issue 3 https://doi.org/10.1016/j.ygeno.2005.05.002	journal	September 2005
Properties of the reversible nonoxidative vanillate / 4-hydroxybenzoate decarboxylase from Bacillus subtilis Lupa, Boguslaw; Lyon, Delina; Shaw, Lindsey N. Canadian Journal of Microbiology, Vol. 54, Issue 1 https://doi.org/10.1139/W07-113	journal	January 2008
New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition Payne, Karl A. P.; White, Mark D.; Fisher, Karl Nature, Vol. 522, Issue 7557 https://doi.org/10.1038/nature14560	journal	June 2015
Biosynthesis and Activity of Prenylated FMN Cofactors Wang, Po-Hsiang; Khusnutdinova, Anna N.; Luo, Fei Cell Chemical Biology, Vol. 25, Issue 5 https://doi.org/10.1016/j.chembiol.2018.02.007	journal	May 2018
Flavoenzymes: Versatile catalysts in biosynthetic pathways Walsh, Christopher T.; Wencewicz, Timothy A. Nat. Prod. Rep., Vol. 30, Issue 1 https://doi.org/10.1039/C2NP20069D	journal	January 2013
Regioselective para -Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase Payer, Stefan E.; Marshall, Stephen A.; Bärland, Natalie Angewandte Chemie International Edition, Vol. 56, Issue 44 https://doi.org/10.1002/anie.201708091	journal	October 2017
The non-oxidative decarboxylation ofp-hydroxybenzoic acid, gentisic acid, protocatechuic acid and gallic acid byKlebsiella aerogenes (Aerobacter aerogenes) Grant, D. J. W.; Patel, J. C. Antonie van Leeuwenhoek, Vol. 35, Issue 1 https://doi.org/10.1007/BF02219153	journal	December 1969
Purification, characterization, and gene cloning of 4-hydroxybenzoate decarboxylase of Enterobacter cloacae P240 Matsui, Tsuyoshi; Yoshida, Toyokazu; Hayashi, Toshihisa Archives of Microbiology, Vol. 186, Issue 1 https://doi.org/10.1007/s00203-006-0117-5	journal	June 2006
Gentisate and 3-oxoadipate pathways in the yeast Candida parapsilosis: identification and functional analysis of the genes coding for 3-hydroxybenzoate 6-hydroxylase and 4-hydroxybenzoate 1-hydroxylase Holesova, Z.; Jakubkova, M.; Zavadiakova, I. Microbiology, Vol. 157, Issue 7 https://doi.org/10.1099/mic.0.048215-0	journal	April 2011
Mechanism of the Salicylate Hydroxylase Reaction Katagiri, Masayuki; Takemori, Shigeki; Suzuki, Kenzi Journal of Biological Chemistry, Vol. 241, Issue 23 https://doi.org/10.1016/S0021-9258(18)96397-0	journal	December 1966
Metabolism of Aromatic Compounds in Bacteria Reiner, Albey M. Journal of Biological Chemistry, Vol. 247, Issue 16 https://doi.org/10.1016/S0021-9258(19)44924-7	journal	August 1972
Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily Neidle, Ellen; Hartnett, Christopher; Ornston, L. Nicholas European Journal of Biochemistry, Vol. 204, Issue 1 https://doi.org/10.1111/j.1432-1033.1992.tb16612.x	journal	February 1992
Metabolism of Benzoic Acid by Bacteria: 3,5- Cyclohexadiene-1,2-Diol-1-Carboxylic Acid Is an Intermediate in the Formation of Catechol Reiner, Albey M. Journal of Bacteriology, Vol. 108, Issue 1 https://doi.org/10.1128/jb.108.1.89-94.1971	journal	October 1971
Catabolic role of a three-component salicylate oxygenase from Sphingomonas yanoikuyae B1 in polycyclic aromatic hydrocarbon degradation Cho, Okyoung; Choi, Ki Young; Zylstra, Gerben J. Biochemical and Biophysical Research Communications, Vol. 327, Issue 3 https://doi.org/10.1016/j.bbrc.2004.12.060	journal	February 2005
Advanced Biotechnology: Metabolically Engineered Cells for the Bio-Based Production of Chemicals and Fuels, Materials, and Health-Care Products Becker, Judith; Wittmann, Christoph Angewandte Chemie International Edition, Vol. 54, Issue 11 https://doi.org/10.1002/anie.201409033	journal	February 2015
Debottlenecking 4-hydroxybenzoate hydroxylation in Pseudomonas putida KT2440 improves muconate productivity from p-coumarate Kuatsjah, Eugene; Johnson, Christopher W.; Salvachúa, Davinia Metabolic Engineering, Vol. 70 https://doi.org/10.1016/j.ymben.2021.12.010	journal	March 2022
Metabolic response of Pseudomonas putida to increased NADH regeneration rates Zobel, Sebastian; Kuepper, Jannis; Ebert, Birgitta Engineering in Life Sciences, Vol. 17, Issue 1 https://doi.org/10.1002/elsc.201600072	journal	October 2016
Discovery of Novel p -Hydroxybenzoate- m -hydroxylase, Protocatechuate 3,4 Ring-Cleavage Dioxygenase, and Hydroxyquinol 1,2 Ring-Cleavage Dioxygenase from the Filamentous Fungus Aspergillus niger Lubbers, Ronnie J. M.; Dilokpimol, Adiphol; Peng, Mao ACS Sustainable Chemistry & Engineering, Vol. 7, Issue 23 https://doi.org/10.1021/acssuschemeng.9b04918	journal	November 2019
Cofactor engineering for more efficient production of chemicals and biofuels Wang, Meng; Chen, Biqiang; Fang, Yunming Biotechnology Advances, Vol. 35, Issue 8 https://doi.org/10.1016/j.biotechadv.2017.09.008	journal	December 2017
Selective oxidative demethylation of veratric acid to vanillic acid by CYP199A4 from Rhodopseudomonas palustris HaA2 Bell, Stephen G.; Tan, Adrian B. H.; Johnson, Eachan O. D. Mol. BioSyst., Vol. 6, Issue 1 https://doi.org/10.1039/B913487E	journal	January 2009
Investigating the effect of available redox protein ratios for the conversion of a steroid by a myxobacterial CYP260A1 Khatri, Yogan; Schifrin, Alexander; Bernhardt, Rita FEBS Letters, Vol. 591, Issue 8 https://doi.org/10.1002/1873-3468.12619	journal	April 2017
Nonrefoldability is Pervasive Across the E. coli Proteome To, Philip; Whitehead, Briana; Tarbox, Haley E. Journal of the American Chemical Society, Vol. 143, Issue 30 https://doi.org/10.1021/jacs.1c03270	journal	July 2021
Development of Engineered Ferredoxin Reductase Systems for the Efficient Hydroxylation of Steroidal Substrates Zhu, Zhangliang; Gao, Xin; Song, Zhan ACS Sustainable Chemistry & Engineering, Vol. 8, Issue 44 https://doi.org/10.1021/acssuschemeng.0c07042	journal	October 2020
New Reactions and Products Resulting from Alternative Interactions between the P450 Enzyme and Redox Partners Zhang, Wei; Liu, Yi; Yan, Jinyong Journal of the American Chemical Society, Vol. 136, Issue 9 https://doi.org/10.1021/ja4130302	journal	February 2014
Co-upgrading of ethanol-assisted depolymerized lignin: A new biological lignin valorization approach for the production of protocatechuic acid and polyhydroxyalkanoic acid Nguyen, Linh Thanh; Tran, My Ha; Lee, Eun Yeol Bioresource Technology, Vol. 338 https://doi.org/10.1016/j.biortech.2021.125563	journal	October 2021
The emergence of adaptive laboratory evolution as an efficient tool for biological discovery and industrial biotechnology Sandberg, Troy E.; Salazar, Michael J.; Weng, Liam L. Metabolic Engineering, Vol. 56 https://doi.org/10.1016/j.ymben.2019.08.004	journal	December 2019
Adaptive laboratory evolution of Pseudomonas putida KT2440 improves p-coumaric and ferulic acid catabolism and tolerance Mohamed, Elsayed T.; Werner, Allison Z.; Salvachúa, Davinia Metabolic Engineering Communications, Vol. 11 https://doi.org/10.1016/j.mec.2020.e00143	journal	December 2020
Outer membrane vesicles catabolize lignin-derived aromatic compounds in Pseudomonas putida KT2440 Salvachúa, Davinia; Werner, Allison Z.; Pardo, Isabel Proceedings of the National Academy of Sciences, Vol. 117, Issue 17 https://doi.org/10.1073/pnas.1921073117	journal	April 2020
Bacterial Nanobioreactors–Directing Enzyme Packaging into Bacterial Outer Membrane Vesicles Alves, Nathan J.; Turner, Kendrick B.; Daniele, Michael A. ACS Applied Materials & Interfaces, Vol. 7, Issue 44 https://doi.org/10.1021/acsami.5b08811	journal	October 2015
The imminent role of protein engineering in synthetic biology Foo, Jee Loon; Ching, Chi Bun; Chang, Matthew Wook Biotechnology Advances, Vol. 30, Issue 3 https://doi.org/10.1016/j.biotechadv.2011.09.008	journal	May 2012
A Growth-Based, High-Throughput Selection Platform Enables Remodeling of 4-Hydroxybenzoate Hydroxylase Active Site Maxel, Sarah; Aspacio, Derek; King, Edward ACS Catalysis, Vol. 10, Issue 12 https://doi.org/10.1021/acscatal.0c01892	journal	June 2020
A protocatechuate biosensor for Pseudomonas putida KT2440 via promoter and protein evolution Jha, Ramesh K.; Bingen, Jeremy M.; Johnson, Christopher W. Metabolic Engineering Communications, Vol. 6 https://doi.org/10.1016/j.meteno.2018.03.001	journal	June 2018
13C Metabolic Flux Analysis Wiechert, Wolfgang Metabolic Engineering, Vol. 3, Issue 3 https://doi.org/10.1006/mben.2001.0187	journal	July 2001
Passive membrane transport of lignin-related compounds Vermaas, Josh V.; Dixon, Richard A.; Chen, Fang Proceedings of the National Academy of Sciences, Vol. 116, Issue 46 https://doi.org/10.1073/pnas.1904643116	journal	October 2019
Characterization of aromatic acid/proton symporters in Pseudomonas putida KT2440 toward efficient microbial conversion of lignin-related aromatics Wada, Ayumu; Prates, Érica T.; Hirano, Ryo Metabolic Engineering, Vol. 64 https://doi.org/10.1016/j.ymben.2021.01.013	journal	March 2021
Engineering the spatial organization of metabolic enzymes: mimicking nature's synergy Conrado, Robert J.; Varner, Jeffrey D.; DeLisa, Matthew P. Current Opinion in Biotechnology, Vol. 19, Issue 5 https://doi.org/10.1016/j.copbio.2008.07.006	journal	October 2008
Spatial organization of enzymes for metabolic engineering Lee, Hanson; DeLoache, William C.; Dueber, John E. Metabolic Engineering, Vol. 14, Issue 3 https://doi.org/10.1016/j.ymben.2011.09.003	journal	May 2012
Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase Entsch, Barrie; Cole, Lindsay J.; Ballou, David P. Archives of Biochemistry and Biophysics, Vol. 433, Issue 1 https://doi.org/10.1016/j.abb.2004.09.029	journal	January 2005
Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts van Berkel, W. J. H.; Kamerbeek, N. M.; Fraaije, M. W. Journal of Biotechnology, Vol. 124, Issue 4 https://doi.org/10.1016/j.jbiotec.2006.03.044	journal	August 2006
Flavin metamorphosis: cofactor transformation through prenylation Leys, David Current Opinion in Chemical Biology, Vol. 47 https://doi.org/10.1016/j.cbpa.2018.09.024	journal	December 2018

Similar Records

The Catabolism of Lignin-Derived p-Methoxylated Aromatic Compounds by Rhodococcus jostii RHA1

Journal Article · 2024 · Applied and Environmental Microbiology · OSTI ID:1855381

Wolf, Megan E.; Lalande, Anne T.; Newman, Brianne L.; +4 more

Elucidation of Aromatic Catabolic Pathways in White-Rot Fungi

Conference · 2021 · OSTI ID:1855381

del Cerro, Carlos; Erickson, Erika; Dong, Tao; +12 more

Outer Membrane Vesicles Catabolize Lignin-Derived Aromatic Compounds in Pseudomonas putida KT2440

Journal Article · 2020 · Proceedings of the National Academy of Sciences of the United States of America · OSTI ID:1855381

Salvachua, Davinia; Werner, Allison Z.; Pardo, Isabel; +16 more

Related Subjects

BIOMASS FUELS,INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
aromatic catabolism
decarboxylation
enzyme
hydroxylation
lignin valorization
metabolic engineering
O-demethylation

Title: Critical Enzyme Reactions in Aromatic Catabolism for Microbial Lignin Conversion

Citation Formats

References (155)

Similar Records

Related Subjects