دورية أكاديمية

Fungal PQQ-dependent dehydrogenases and their potential in biocatalysis.

التفاصيل البيبلوغرافية
العنوان: Fungal PQQ-dependent dehydrogenases and their potential in biocatalysis.
المؤلفون: Takeda K; Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan., Umezawa K; Department of Applied Biological Chemistry, Kindai University, Nara 631-8505, Japan., Várnai A; Faculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway., Eijsink VG; Faculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway., Igarashi K; Department of Biomaterial Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan., Yoshida M; Department of Environmental and Natural Resource Science, Tokyo University of Agriculture and Technology, Fuchu, Tokyo 183-8509, Japan. Electronic address: ymakoto@cc.tuat.ac.jp., Nakamura N; Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan.
المصدر: Current opinion in chemical biology [Curr Opin Chem Biol] 2019 Apr; Vol. 49, pp. 113-121. Date of Electronic Publication: 2018 Dec 20.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't; Review
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: England NLM ID: 9811312 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0402 (Electronic) Linking ISSN: 13675931 NLM ISO Abbreviation: Curr Opin Chem Biol Subsets: MEDLINE
أسماء مطبوعة: Publication: London : Elsevier
Original Publication: London : Current Biology Ltd., c1997-
مواضيع طبية MeSH: Biocatalysis*, Basidiomycota/*enzymology , Oxidoreductases/*metabolism , PQQ Cofactor/*metabolism, Arabinose/metabolism ; Fucose/metabolism ; Galactose/metabolism ; Ketoses/metabolism ; Oxidation-Reduction ; Substrate Specificity
مستخلص: In 2014, the first fungal pyrroloquinoline-quinone (PQQ)-dependent enzyme was discovered as a pyranose dehydrogenase from the basidiomycete Coprinopsis cinerea (CcPDH). This discovery laid the foundation for a new Auxiliary Activities (AA) family, AA12, in the Carbohydrate-Active enZymes (CAZy) database and revealed a novel enzymatic activity potentially involved in biomass conversion. This review summarizes recent progress made in research on this fungal oxidoreductase and related enzymes. CcPDH consists of the catalytic PQQ-binding AA12 domain, an N-terminal cytochrome b AA8 domain, and a C-terminal family 1 carbohydrate-binding module (CBM1). CcPDH oxidizes 2-keto-d-glucose (d-glucosone), l-fucose, and rare sugars such as d-arabinose and l-galactose, and can activate lytic polysaccharide monooxygenases (LPMOs). Bioinformatic studies suggest a widespread occurrence of quinoproteins in eukaryotes as well as prokaryotes.
(Copyright © 2018 Elsevier Ltd. All rights reserved.)
المشرفين على المادة: 0 (Ketoses)
26345-59-5 (glucosone)
28RYY2IV3F (Fucose)
72909-34-3 (PQQ Cofactor)
B40ROO395Z (Arabinose)
EC 1.- (Oxidoreductases)
X2RN3Q8DNE (Galactose)
تواريخ الأحداث: Date Created: 20181224 Date Completed: 20191213 Latest Revision: 20191217
رمز التحديث: 20240628
DOI: 10.1016/j.cbpa.2018.12.001
PMID: 30580186
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0402
DOI:10.1016/j.cbpa.2018.12.001