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Dirigent protein subfamily function and structure in terrestrial plant phenol metabolism.
Meng, Qingyan; Kim, Sung-Jin; Costa, Michael A; Moinuddin, Syed G A; Celoy, Rhodesia M; Smith, Clyde A; Cort, John R; Davin, Laurence B; Lewis, Norman G.
Afiliación
  • Meng Q; Institute of Biological Chemistry, Washington State University, Pullman, WA, United States.
  • Kim SJ; Institute of Biological Chemistry, Washington State University, Pullman, WA, United States.
  • Costa MA; Institute of Biological Chemistry, Washington State University, Pullman, WA, United States.
  • Moinuddin SGA; Institute of Biological Chemistry, Washington State University, Pullman, WA, United States.
  • Celoy RM; School of Plant Sciences, University of Arizona, Tucson, AZ, United States.
  • Smith CA; Stanford Synchrotron Radiation Lightsource, Menlo Park, CA, United States.
  • Cort JR; Institute of Biological Chemistry, Washington State University, Pullman, WA, United States; Earth and Biological Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA, United States.
  • Davin LB; Institute of Biological Chemistry, Washington State University, Pullman, WA, United States.
  • Lewis NG; Institute of Biological Chemistry, Washington State University, Pullman, WA, United States. Electronic address: lewisn@wsu.edu.
Methods Enzymol ; 683: 101-150, 2023.
Article en En | MEDLINE | ID: mdl-37087184
Aquatic plant transition to land, and subsequent terrestrial plant species diversification, was accompanied by the emergence and massive elaboration of plant phenol chemo-diversity. Concomitantly, dirigent protein (DP) and dirigent-like protein subfamilies, derived from large multigene families, emerged and became extensively diversified. DP biochemical functions as gateway entry points into new and diverse plant phenol skeletal types then markedly expanded. DPs have at least eight non-uniformly distributed subfamilies, with different DP subfamily members of known biochemical/physiological function now implicated as gateway entries to lignan, lignin, aromatic diterpenoid, pterocarpan and isoflavene pathways. While some other DP subfamily members have jacalin domains, both these and indeed the majority of DPs throughout the plant kingdom await discovery of their biochemical roles. Methods and approaches were developed to discover DP biochemical function as gateway entry points to distinct plant phenol skeletal types in land plants. Various DP 3D X-ray structural determinations enabled structure-based comparative sequence analysis and modeling to understand similarities and differences among the different DP subfamilies. We consider that the core DP ß-barrel fold and associated characteristics are likely common to all DPs, with several residues conserved and nearly invariant. There is also considerable variation in residue composition and topography of the putative substrate binding pockets, as well as substantial differences in several loops, such as the ß1-ß2 loop. All DPs likely bind and stabilize quinone methide intermediates, while guiding distinctive regio- and/or stereo-chemical entry into Nature's chemo-diverse land plant phenol metabolic classes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fenoles / Plantas Tipo de estudio: Prognostic_studies Idioma: En Revista: Methods Enzymol Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fenoles / Plantas Tipo de estudio: Prognostic_studies Idioma: En Revista: Methods Enzymol Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos