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Difference between revisions of "Glycoside Hydrolase Family 37"
| Line 43: | Line 43: | ||
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | The only structural representative from GH37 to date is the trehalase from ''Escherichia coli'', which was solved using X-ray crystallography <cite>REF1</cite>. The structure revealed a (α/α)6 barrel fold, and was placed into clan GH-G. Structures have been solved with the inhibitors validoxylamine A, 1-thiatrehazolin and a casuarine analogue <cite>REF1;REF2</cite> | |
| Line 50: | Line 50: | ||
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>MikesClassic</cite>. | ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>MikesClassic</cite>. | ||
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>. | ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>. | ||
| − | ;First 3-D structure: | + | ;First 3-D structure: The GH37 trehalase from ''Escherichia coli'' was solved by X-ray crystallography <cite>REF1</cite>. |
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #REF1 pmid=17455176 |
| − | # | + | #REF2 pmid=19123216 |
| − | |||
| − | |||
</biblio> | </biblio> | ||
Revision as of 15:20, 2 October 2009
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: ^^^Tracey Gloster^^^
- Responsible Curator: ^^^Gideon Davies^^^
| Glycoside Hydrolase Family GH37 | |
| Clan | GH-G |
| Mechanism | Inverting |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH37.html | |
Substrate specificities
Content is to be added here.
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
The only structural representative from GH37 to date is the trehalase from Escherichia coli, which was solved using X-ray crystallography [5]. The structure revealed a (α/α)6 barrel fold, and was placed into clan GH-G. Structures have been solved with the inhibitors validoxylamine A, 1-thiatrehazolin and a casuarine analogue [5, 6]
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 [4].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First 3-D structure
- The GH37 trehalase from Escherichia coli was solved by X-ray crystallography [5].
References
- Gibson RP, Gloster TM, Roberts S, Warren RA, Storch de Gracia I, García A, Chiara JL, and Davies GJ. (2007). Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors. Angew Chem Int Ed Engl. 2007;46(22):4115-9. DOI:10.1002/anie.200604825 |
- Cardona F, Parmeggiani C, Faggi E, Bonaccini C, Gratteri P, Sim L, Gloster TM, Roberts S, Davies GJ, Rose DR, and Goti A. (2009). Total syntheses of casuarine and its 6-O-alpha-glucoside: complementary inhibition towards glycoside hydrolases of the GH31 and GH37 families. Chemistry. 2009;15(7):1627-36. DOI:10.1002/chem.200801578 |
[[Category:Glycoside Hydrolase Families|GHnnn]]