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Glycoside Hydrolase Family 97

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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 GH97
Clan Not assigned
Mechanism Retaining and Inverting
Active site residues Inferred
CAZy DB link
http://www.cazy.org/fam/GH97.html


Substrate specificities

Family 97 glycoside hydrolases hydrolyse alpha-linked substrates; the two enzymes from this family that have been characterised to date have alpha-glucosidase (EC 3.2.1.20) and alpha-galactosidase (EC 3.2.1.22) activity [1]. The alpha-glucosidase from Bacteroides thetaiotaomicron has been characterised in the most detail, and has been demonstrated to hydrolyse substrates ranging from maltose to maltoheptaose in length, and those containing alpha-1,6-, alpha-1,3- and alpha-1,2-, as well as alpha-1,4-, linkages [2, 3].

Kinetics and Mechanism

Family GH97 is unusual as it contains both retaining and inverting enzymes, as shown unequivocally by NMR [1] and HPLC [2], by characterization of two enzymes from Bacteroides thetaiotaomicron. Both mechanisms are strongly dependent on the presence of calcium, which coordinates the C2-OH group of the substrate in the -1 subsite, as well as four glutamate residues in the active site [1]. One of the glutamate residues coordinated by the calcium ion is predicted to be the acid/base residue, which may receive acid assistance from the calcium during hydrolysis.

Catalytic Residues

Content is to be added here.


Three-dimensional structures

Content is to be added here.


Family Firsts

First sterochemistry determination
Cite some reference here, with a short (1-2 sentence) explanation [4].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [5].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [6].
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation [7].

References

  1. Gloster TM, Turkenburg JP, Potts JR, Henrissat B, and Davies GJ. (2008). Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora. Chem Biol. 2008;15(10):1058-67. DOI:10.1016/j.chembiol.2008.09.005 | PubMed ID:18848471 [REF1]
  2. Smith KA and Salyers AA. (1991). Characterization of a neopullulanase and an alpha-glucosidase from Bacteroides thetaiotaomicron 95-1. J Bacteriol. 1991;173(9):2962-8. DOI:10.1128/jb.173.9.2962-2968.1991 | PubMed ID:1708385 [REF2]
  3. Kitamura M, Okuyama M, Tanzawa F, Mori H, Kitago Y, Watanabe N, Kimura A, Tanaka I, and Yao M. (2008). Structural and functional analysis of a glycoside hydrolase family 97 enzyme from Bacteroides thetaiotaomicron. J Biol Chem. 2008;283(52):36328-37. DOI:10.1074/jbc.M806115200 | PubMed ID:18981178 [REF3]

All Medline abstracts: PubMed

[[Category:Glycoside Hydrolase Families|GHnnn]]