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Difference between revisions of "Glycoside Hydrolase Family 124"
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== 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>. | |
This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. | This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. | ||
| Line 54: | Line 54: | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Bras2011 pmid=21393568 |
#He1999 pmid=9312086 | #He1999 pmid=9312086 | ||
#StickWilliams isbn=978-0-240-52118-3 | #StickWilliams isbn=978-0-240-52118-3 | ||
Revision as of 03:42, 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 | |
| https://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].
This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].
Kinetics and Mechanism
Content is to be added here.
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 [4].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [3].
References
- 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 |
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Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- 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 |