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Glycoside Hydrolase Family 145

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This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.

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This family has been deleted from the CAZy classification. A specific explanation may be found below.

GH145 is a deleted family

This family has been reclassified as Polysaccharide Lyase Family 42. Two members of the family from Bacteroides species were originally shown to have hydrolase activity catalyzed by a semi-conserved active site on the posterior side of the beta-propeller structure [1]. Subsequently, lyase activity on alpha-L-Rha-1,4-alpha-D-GlcA via a well-conserved active site on the anterior surface, with strong similarity to PL24 and PL25, was demonstrated in fungal [2] and bacterial [3] homologs.


  1. Munoz-Munoz J, Cartmell A, Terrapon N, Henrissat B, and Gilbert HJ. (2017). Unusual active site location and catalytic apparatus in a glycoside hydrolase family. Proc Natl Acad Sci U S A. 2017;114(19):4936-4941. DOI:10.1073/pnas.1701130114 | PubMed ID:28396425 [MunozMunoz2017]
  2. Kondo T, Kichijo M, Maruta A, Nakaya M, Takenaka S, Arakawa T, Fushinobu S, and Sakamoto T. (2021). Structural and functional analysis of gum arabic l-rhamnose-α-1,4-d-glucuronate lyase establishes a novel polysaccharide lyase family. J Biol Chem. 2021;297(3):101001. DOI:10.1016/j.jbc.2021.101001 | PubMed ID:34303708 [Kondo2021]
  3. Munoz-Munoz J, Ndeh D, Fernandez-Julia P, Walton G, Henrissat B, and Gilbert HJ. (2021). Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius. mBio. 2021;12(4):e0136821. DOI:10.1128/mBio.01368-21 | PubMed ID:34340552 [MunozMunoz2021]

All Medline abstracts: PubMed

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