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Glycoside Hydrolase Family 106

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Glycoside Hydrolase Family GH106
Clan none
Mechanism inverting
Active site residues known
CAZy DB link
https://www.cazy.org/GH106.html


Substrate specificities

The glycoside hydrolases of this family are alfa L-rhamnosidases (EC 3.2.1.40). The first GH106 characterized was Rham from Sphingomonas paucimobilis FP2001. This enzyme showed activity against p-nitrophenyl α-L-rhamnopyranoside. More recently, two Bacteroides thetaiotaomicron enzymes (BT0986 and BT4145) have been characterized. These enzymes are exo active against linkages present in pectin polysaccharides. BT0986 cleaves the L-Rha-a-1,2-L-Arap linkage in the terminal region of Chain B of rhamnogalacturonan II. The enzyme BT4145 targets the L-Rha-a-1,4-D-GalA linkage in the backbone of rhamnogalacturonan I. All of genes encoding family 106 members are found in bacteria.

In the meantime, please see these references for an essential introduction to the CAZy classification system: [1, 2].

Kinetics and Mechanism

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Catalytic Residues

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Three-dimensional structures

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Family Firsts

First stereochemistry determination
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First catalytic nucleophile identification
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First general acid/base residue identification
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First 3-D structure
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References

  1. Miyata T, Kashige N, Satho T, Yamaguchi T, Aso Y and Miake F.Cloning (2005) Sequence analysis, and expression of the gene encoding Sphingomonas paucimobilis FP2001 alpha-L-rhamnosidase. Curr Microbiol, vol 51, no. 2., pp. 105-109.

    [Miyata2005]
  2. Ndeh D, Rogowski A, Cartmell A, Luis AS, Baslé A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neil MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, and Gilbert HJ. (2017). Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature. 2017;544(7648):65-70. DOI:10.1038/nature21725 | PubMed ID:28329766 [Ndeh2017]
  3. Luis AS, Briggs J, Zhang X, Farnell B, Ndeh D, Labourel A, Baslé A, Cartmell A, Terrapon N, Stott K, Lowe EC, McLean R, Shearer K, Schückel J, Venditto I, Ralet MC, Henrissat B, Martens EC, Mosimann SC, Abbott DW, and Gilbert HJ. (2018). Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides. Nat Microbiol. 2018;3(2):210-219. DOI:10.1038/s41564-017-0079-1 | PubMed ID:29255254 [Luis2018]

All Medline abstracts: PubMed