pHBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar

Autor: Lisanne de Vries, Heather A MacKay, Rebecca A Smith, Yaseen Mottiar, Steven D Karlen, Faride Unda, Emilia Muirragui, Craig Bingman, Kirk Vander Meulen, Emily T Beebe, Brian G Fox, John Ralph, Shawn D Mansfield

Publikováno v: Plant Physiology. 188:1014-1027

Poplar (Populus) lignin is naturally acylated with p-hydroxybenzoate ester moieties. However, the enzyme(s) involved in the biosynthesis of the monolignol–p-hydroxybenzoates have remained largely unknown. Here, we performed an in vitro screen of th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44450a7fd0bf97f6b926f691b0a4b0e8
https://doi.org/10.1093/plphys/kiab546

Mannose- and Mannobiose-Specific Responses of the Insect-Associated Cellulolytic Bacterium Streptomyces sp. Strain SirexAA-E

Autor: Natsumi Kato, Taichi E. Takasuka, Wakana Sato, Emily T. Beebe, Cameron R. Currie, Keisuke Ohashi, Akane Nakata, Kazuki Matsumoto, Camila Carlos-Shanley, Brian G. Fox, Shogo Hataya

Publikováno v: Applied and Environmental Microbiology. 87

The cellulolytic insect symbiont bacterium Streptomyces sp. strain SirexAA-E secretes a suite of carbohydrate-active enzymes (CAZymes), which are involved in the degradation of various polysaccharides in the plant cell wall, in response to the availa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57540a2042c5c080d872f3b6e6ce7f76
https://doi.org/10.1128/aem.02719-20

Mannose- and Mannobiose-Specific Responses of the Insect-Associated Cellulolytic Bacterium

Autor: Keisuke, Ohashi, Shogo, Hataya, Akane, Nakata, Kazuki, Matsumoto, Natsumi, Kato, Wakana, Sato, Camila, Carlos-Shanley, Emily T, Beebe, Cameron R, Currie, Brian G, Fox, Taichi E, Takasuka

Publikováno v: Appl Environ Microbiol

The cellulolytic insect symbiont bacterium Streptomyces sp. strain SirexAA-E secretes a suite of carbohydrate-active enzymes (CAZymes), which are involved in the degradation of various polysaccharides in the plant cell wall, in response to the availa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f1bb227c0761f6434fe2061565d6ac59
https://pubmed.ncbi.nlm.nih.gov/33990299

A heterodimeric glutathione

Autor: Wayne S, Kontur, Charles N, Olmsted, Larissa M, Yusko, Alyssa V, Niles, Kevin A, Walters, Emily T, Beebe, Kirk A, Vander Meulen, Steven D, Karlen, Daniel L, Gall, Daniel R, Noguera, Timothy J, Donohue

Publikováno v: The Journal of Biological Chemistry

Lignin is a heterogeneous polymer of aromatic subunits that is a major component of lignocellulosic plant biomass. Understanding how microorganisms deconstruct lignin is important for understanding the global carbon cycle and could aid in developing

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d8141e345ba02d55d94f7fb5d44b9826
https://pubmed.ncbi.nlm.nih.gov/30541921

Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling

Autor: Maryam Mirzai, Michael G. Hahn, Johnnie A. Walker, Emily T. Beebe, Lai F. Bergeman, Sivakumar Pattathil, Kai Deng, Brian G. Fox, Trent R. Northen

Publikováno v: Walker, JA; Pattathil, S; Bergeman, LF; Beebe, ET; Deng, K; Mirzai, M; et al.(2017). Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling. Biotechnology for Biofuels, 10(1). doi: 10.1186/s13068-017-0703-6. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/0z0563wg
Biotechnology for biofuels, vol 10, iss 1
Biotechnology for Biofuels

Background Glycoside hydrolases (GHs) are enzymes that hydrolyze polysaccharides into simple sugars. To better understand the specificity of enzyme hydrolysis within the complex matrix of polysaccharides found in the plant cell wall, we studied the r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e01d2f54e586b2f5559a13603bd583a
https://doi.org/10.1186/s13068-017-0703-6