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Difference between revisions of "Syn/anti lateral protonation"
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This table can be re-sorted by clicking on the icons in the header (''javascript must be turned on in your browser''). To reset the page to be sorted by GH family, click the ''page'' above the page title. | This table can be re-sorted by clicking on the icons in the header (''javascript must be turned on in your browser''). To reset the page to be sorted by GH family, click the ''page'' above the page title. | ||
{| cellspacing="0" cellpadding="4" border="0" class="sortable" | {| cellspacing="0" cellpadding="4" border="0" class="sortable" | ||
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! '''Family''' | ! '''Family''' | ||
! '''Anomeric specificity''' | ! '''Anomeric specificity''' | ||
Revision as of 00:23, 9 November 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: ^^^Wim Nerinckx^^^
- Responsible Curator: ^^^Spencer Williams^^^
Overview
This page will provide a table and eventually a full lexicon article on the spatial positioning of the catalytic general acid residue in the active sites of glycoside hydrolases. The table below updates those found in the seminal paper on this concept by Heightman and Vasella [1], and the more recent summary by Nerinckx et al. [2].
Table
This table can be re-sorted by clicking on the icons in the header (javascript must be turned on in your browser). To reset the page to be sorted by GH family, click the page above the page title.
| Family | Anomeric specificity | Mechanism | General acid | syn/anti | Nucleophile or General base |
Ligand | Organism | Enzyme | PDB ID | Primary reference |
|---|---|---|---|---|---|---|---|---|---|---|
| GH1 | beta | retaining | Glu160 | anti | Glu375 | product | Lactococcus lactis | 6-phosopho-beta-galactosidase | 4pbg | [3] |
| GH9 | beta | inverting | Glu424 | anti | Asp55,Asp58 | product | Thermomonospora fusca | cellulase | 3tf4,4tf4 | [4] |
References
-
Heightman, T.D. and Vasella, A.T. (1999) Recent Insights into Inhibition, Structure, and Mechanism of Configuration-Retaining Glycosidases. Angewandte Chemie-International Edition 38(6), 750-770. Article online.
- Nerinckx W, Desmet T, Piens K, and Claeyssens M. (2005). An elaboration on the syn-anti proton donor concept of glycoside hydrolases: electrostatic stabilisation of the transition state as a general strategy. FEBS Lett. 2005;579(2):302-12. DOI:10.1016/j.febslet.2004.12.021 |
- Wiesmann C, Hengstenberg W, and Schulz GE. (1997). Crystal structures and mechanism of 6-phospho-beta-galactosidase from Lactococcus lactis. J Mol Biol. 1997;269(5):851-60. DOI:10.1006/jmbi.1997.1084 |
- Irwin D, Shin DH, Zhang S, Barr BK, Sakon J, Karplus PA, and Wilson DB. (1998). Roles of the catalytic domain and two cellulose binding domains of Thermomonospora fusca E4 in cellulose hydrolysis. J Bacteriol. 1998;180(7):1709-14. DOI:10.1128/JB.180.7.1709-1714.1998 |