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Difference between revisions of "Glycoside Hydrolase Family 145"
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| − | * [[Responsible Curator]]: | + | * [[Author]]: [[User:Harry Brumer|Harry Brumer]] |
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| + | * [[Responsible Curator]]: [[User:Bernard Henrissat|Bernard Henrissat]] | ||
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=== GH145 is a deleted family === | === GH145 is a deleted family === | ||
| − | This family has been reclassified as [[Polysaccharide Lyase Family 42]]. | + | 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 <cite>MunozMunoz2017</cite>. 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 <cite>Kondo2021</cite> and bacterial <cite>MunozMunoz2021</cite> homologs. |
'''References''' | '''References''' | ||
<biblio> | <biblio> | ||
| + | #MunozMunoz2017 pmid=28396425 | ||
| + | #MunozMunoz2021 pmid=34340552 | ||
| + | #Kondo2021 pmid=34303708 | ||
</biblio> | </biblio> | ||
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --> | <!-- The data in the table below should be updated by the Author/Curator according to current information on the family --> | ||
Latest revision as of 14:15, 18 December 2021
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.
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.
References
- 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 |
- 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 |
- 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 |
| CAZy DB links | |
| http://www.cazy.org/GH145.html | |
| http://www.cazy.org/PL42.html |