New to the CAZy classification? Read this first.
Want to learn more about CAZypedia? Read the CAZypedia 10th anniversary article in Glycobiology.

Glycoside Hydrolase Family 45

From CAZypedia
Revision as of 23:48, 5 October 2010 by Harry Brumer (Talk | contribs) (minor touch-up of cite tags)
Jump to: navigation, search
Under construction icon-blue-48px.png
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 GH45
Clan none
Mechanism inverting
Active site residues known (but see discussion)
CAZy DB link

Substrate specificities

Glycoside hydrolases of GH45 are endoglucanases (EC; mainly the hydrolysis of soluble β -1,4 glucans.

Kinetics and Mechanism

The enzymes, formally known as cellulase family "K" in some historic literature, act with inversion of anomeric configuration to generate the α-D anomer of the oligosaccaride as product. Based upon the structure of the Humicola insolens endoglucanase V (now known as Cel45)[1, 2] it was concluded that Asp121 acted as the general acid (implied by its hydrogen bonding to the glycosidic oxygen of a ligand in the +1 subsite) and that the most likely general base is Asp10, appropriately positioned "below" the sugar plane. As with many inverting enzymes the base assignment is less secure than that of the acid.

Catalytic Residues

"Classical" GH45 enzymes likely use twin carboxylates corresponding to Asp10 and 121 of the Humicola insolens endoglucanase V [1][2].

Three-dimensional structures

The 3-D structure of canonical GH45 enzymes is a six-stranded β-barrel to which a seventh strand is appended. The structure differs from classical β-barrels in containing both parallel and anti-parallel β-strands. At the time of the first structure solution the fold had ony previously been observed in "Barwin" [3]; a plant defense protein of unknown function. As is now expected for endo-enzymes, the active centre is located in an open substrate-binding groove. The original uncomplexes native structure had an disordered loop above the active centre and this was only seen to become ordered subsequently upon the binding of cello-oligosaccharides [2].

Family GH45 enzymes are structurally related to plant [4] and bacterial [5] expansins. Indeed they even display some of the catalytic centre motifs such as the catalytic acid. The putative catalytic base is absent in expansins.

Family Firsts

First sterochemistry determination
As part of an analysis of many families reported in [6].
First general acid/base residue identification
Catalytic residue proposals have been made solely on the basis of 3-D structure [1, 2].
First 3-D structure
The Humicola insolens EGV (now Cel45) by the Davies group [1].


  1. Davies GJ, Dodson GG, Hubbard RE, Tolley SP, Dauter Z, Wilson KS, Hjort C, Mikkelsen JM, Rasmussen G, and Schülein M. (1993) Structure and function of endoglucanase V. Nature. 365, 362-4. DOI:10.1038/365362a0 | PubMed ID:8377830 | HubMed [Davies1993]
  2. Davies GJ, Tolley SP, Henrissat B, Hjort C, and Schülein M. (1995) Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 A resolution. Biochemistry. 34, 16210-20. PubMed ID:8519779 | HubMed [Davies1995]
  3. Ludvigsen S and Poulsen FM. (1992) Three-dimensional structure in solution of barwin, a protein from barley seed. Biochemistry. 31, 8783-9. PubMed ID:1390665 | HubMed [Ludvigsen]
  4. Yennawar NH, Li LC, Dudzinski DM, Tabuchi A, and Cosgrove DJ. (2006) Crystal structure and activities of EXPB1 (Zea m 1), a beta-expansin and group-1 pollen allergen from maize. Proc Natl Acad Sci U S A. 103, 14664-71. DOI:10.1073/pnas.0605979103 | PubMed ID:16984999 | HubMed [Yennawar]
  5. Kerff F, Amoroso A, Herman R, Sauvage E, Petrella S, Filée P, Charlier P, Joris B, Tabuchi A, Nikolaidis N, and Cosgrove DJ. (2008) Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization. Proc Natl Acad Sci U S A. 105, 16876-81. DOI:10.1073/pnas.0809382105 | PubMed ID:18971341 | HubMed [Kerff]
  6. Schou C, Rasmussen G, Kaltoft MB, Henrissat B, and Schülein M. (1993) Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases. Eur J Biochem. 217, 947-53. PubMed ID:8223652 | HubMed [Schou93]
All Medline abstracts: PubMed | HubMed