CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.

Difference between revisions of "Glycoside Hydrolase Family 53"

From CAZypedia
Jump to navigation Jump to search
Line 38: Line 38:
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
Content is to be added here.
+
As for all members of Clan GH-A (ref), GH53 displays a (beta/alpha)8 barrel structure for the catalytic domain, usually with fairly compact loop structure (ref) and a size range... A disulphide bridging two loops in 3 known fungal structures, is replaced functionally by a calcium ion in one bacterial structure (refs). In most cases the catalytic domain is found in isolation, and not accompanied by accessory domains, but some exceptions exist (refs). For one bacterial member of the family ligand complexes with products have been obtained crystallographically, occupying subsites -4 to -2 and +1 to +2 (refs). Based on these crystal structures, binding of a galactononaose fragment has also been computationally modelled (ref).
 
 
  
 
== Family Firsts ==
 
== Family Firsts ==

Revision as of 00:17, 12 January 2010

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 GH53
Clan GH-A
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/fam/GH53.html


Substrate specificities

The only known specificity for this family is beta-1,4-galactanase (EC 3.2.1.89) and the only reported function is the microbial degradation of galactans and arabinogalactans in the pectic component of plant cell walls. A number of patents on industrial applications of GH53 have been filed.

Kinetics and Mechanism

GH53 beta-1,4-galactanases follow a classical retaining mechanism (Ref.). Most characterized members have been reported to have an endo-mode of action (refs), although processivity has been suggested in one case (Ref).

Catalytic Residues

Two glutamates act as catalytic residues, as nucleophile and acid-base catalyst respectively, and were first identified by Braithwhite et al,.

Three-dimensional structures

As for all members of Clan GH-A (ref), GH53 displays a (beta/alpha)8 barrel structure for the catalytic domain, usually with fairly compact loop structure (ref) and a size range... A disulphide bridging two loops in 3 known fungal structures, is replaced functionally by a calcium ion in one bacterial structure (refs). In most cases the catalytic domain is found in isolation, and not accompanied by accessory domains, but some exceptions exist (refs). For one bacterial member of the family ligand complexes with products have been obtained crystallographically, occupying subsites -4 to -2 and +1 to +2 (refs). Based on these crystal structures, binding of a galactononaose fragment has also been computationally modelled (ref).

Family Firsts

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

References

  1. Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H, and Kelly RM. (2007). Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry. 2007;46(11):3319-30. DOI:10.1021/bi061521n | PubMed ID:17323919 [Comfort2007]
  2. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006

    [MikesClassic]
  3. He S and Withers SG. (1997). Assignment of sweet almond beta-glucosidase as a family 1 glycosidase and identification of its active site nucleophile. J Biol Chem. 1997;272(40):24864-7. DOI:10.1074/jbc.272.40.24864 | PubMed ID:9312086 [He1999]
  4. [3]

All Medline abstracts: PubMed