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Multiplicity of enzymatic functions in the CAZy AA3 family

Journal

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 102, Issue 6, Pages 2477-2492

Publisher

SPRINGER
DOI: 10.1007/s00253-018-8784-0

Keywords

Cellobiose dehydrogenase; Glucose oxidase; Aryl-alcohol oxidase; Methanol oxidase; Pyranose oxidase; Glucose dehydrogenase; Lignocellulose degradation

Funding

  1. Austrian Science Fund (FWF)
  2. Austrian Science Fund (FWF) Doctoral Programme BioToP-Biomolecular Technology of Proteins [FWFW1224]
  3. European Union's Horizon 2020 research and innovation program (ERC Consolidator Grant OXIDIZE) [726396]
  4. Technology Grant Southeast Asia scholarship
  5. ASEAN-European Academic University Network (ASEA-UNINET)
  6. Austrian Federal Ministry of Science, Research and Economy
  7. Austrian Agency for International Cooperation in Education and Research (OeAD-GmbH)

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The CAZy auxiliary activity family 3 (AA3) comprises enzymes from the glucose-methanol-choline (GMC) family of oxidoreductases, which assist the activity of other AA family enzymes via their reaction products or support the action of glycoside hydrolases in lignocellulose degradation. The AA3 family is further divided into four subfamilies, which include cellobiose dehydrogenase, glucose oxidoreductases, aryl-alcohol oxidase, alcohol (methanol) oxidase, and pyranose oxidoreductases. These different enzymes catalyze a wide variety of redox reactions with respect to substrates and co-substrates. The common feature of AA3 family members is the formation of key metabolites such as H2O2 or hydroquinones, which are required by other AA enzymes. The multiplicity of enzymatic functions in the AA3 family is reflected by the multigenicity of AA3 genes in fungi, which also depends on their lifestyle. We provide an overview of the phylogenetic, molecular, and catalytic properties of AA3 enzymes and discuss their interactions with other carbohydrate-active enzymes.

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