CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
*
Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.
Difference between revisions of "Glycoside Hydrolase Family 124"
| Line 30: | Line 30: | ||
== Substrate specificities == | == Substrate specificities == | ||
Family 124 consists of a small number of cellulosomal proteins. The ''Clostridium thermocellum'' enzyme CtCel124A is the only member of this family that has been characterized. The enzyme is an endo-beta1,4-glucanase with modest activity in vitro, but acts in synergy with the major exo-cellulase from ''C. thermocellum'' and, as a discrete entity, is able to deconstruct tobacco cell walls <cite>Comfort2007</cite>. | Family 124 consists of a small number of cellulosomal proteins. The ''Clostridium thermocellum'' enzyme CtCel124A is the only member of this family that has been characterized. The enzyme is an endo-beta1,4-glucanase with modest activity in vitro, but acts in synergy with the major exo-cellulase from ''C. thermocellum'' and, as a discrete entity, is able to deconstruct tobacco cell walls <cite>Comfort2007</cite>. | ||
| − | |||
| − | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | HPLC using cellopentaose as the substrate showed that the enzyme has a single displacement inverting mechanism <cite>Comfort2007</cite>. | |
| + | . | ||
Revision as of 04:45, 27 April 2012
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.
- Author: ^^^Harry Gilbert^^^
- Responsible Curator: ^^^Harry Gilbert^^^
| Glycoside Hydrolase Family GH124 | |
| Clan | GH-x |
| Mechanism | retaining/inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| http://www.cazy.org/GH124.html | |
Substrate specificities
Family 124 consists of a small number of cellulosomal proteins. The Clostridium thermocellum enzyme CtCel124A is the only member of this family that has been characterized. The enzyme is an endo-beta1,4-glucanase with modest activity in vitro, but acts in synergy with the major exo-cellulase from C. thermocellum and, as a discrete entity, is able to deconstruct tobacco cell walls [1].
Kinetics and Mechanism
HPLC using cellopentaose as the substrate showed that the enzyme has a single displacement inverting mechanism [1]. .
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry 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
-
Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- 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 |
- Robert V. Stick and Spencer J. Williams. (2009) Carbohydrates. Elsevier Science.
- Brás JL, Cartmell A, Carvalho AL, Verzé G, Bayer EA, Vazana Y, Correia MA, Prates JA, Ratnaparkhe S, Boraston AB, Romão MJ, Fontes CM, and Gilbert HJ. (2011). Structural insights into a unique cellulase fold and mechanism of cellulose hydrolysis. Proc Natl Acad Sci U S A. 2011;108(13):5237-42. DOI:10.1073/pnas.1015006108 |