1h6m
From Proteopedia
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| - | [[Image:1h6m.gif|left|200px]]<br /> | + | [[Image:1h6m.gif|left|200px]]<br /><applet load="1h6m" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1h6m" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1h6m, resolution 1.64Å" /> | caption="1h6m, resolution 1.64Å" /> | ||
'''COVALENT GLYCOSYL-ENZYME INTERMEDIATE OF HEN EGG WHITE LYSOZYME'''<br /> | '''COVALENT GLYCOSYL-ENZYME INTERMEDIATE OF HEN EGG WHITE LYSOZYME'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H6M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | + | 1H6M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Known structural/functional Sites: <scene name='pdbsite=NA:Na Binding Site For Chain A'>NA</scene>, <scene name='pdbsite=NAG:Nag Binding Site For Chain A'>NAG</scene> and <scene name='pdbsite=NUC:The Covalent Intermediate Is Linked To The Enzynmatic Nu ...'>NUC</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H6M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: mechanism]] | [[Category: mechanism]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:04:03 2007'' |
Revision as of 13:54, 18 December 2007
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COVALENT GLYCOSYL-ENZYME INTERMEDIATE OF HEN EGG WHITE LYSOZYME
Overview
Hen egg-white lysozyme (HEWL) was the first enzyme to have its, three-dimensional structure determined by X-ray diffraction techniques. A, catalytic mechanism, featuring a long-lived oxocarbenium-ion intermediate, was proposed on the basis of model-building studies. The 'Phillips', mechanism is widely held as the paradigm for the catalytic mechanism of, beta-glycosidases that cleave glycosidic linkages with net retention of, configuration of the anomeric centre. Studies with other retaining, beta-glycosidases, however, provide strong evidence pointing to a common, mechanism for these enzymes that involves a covalent glycosyl-enzyme, intermediate, as previously postulated. Here we show, in three different, cases using electrospray ionization mass spectrometry, a catalytically, competent covalent glycosyl-enzyme intermediate during the catalytic cycle, of HEWL. We also show the three-dimensional structure of this intermediate, as determined by X-ray diffraction. We formulate a general catalytic, mechanism for all retaining beta-glycosidases that includes substrate, distortion, formation of a covalent intermediate, and the electrophilic, migration of C1 along the reaction coordinate.
About this Structure
1H6M is a Single protein structure of sequence from Gallus gallus with NA as ligand. Active as Lysozyme, with EC number 3.2.1.17 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate., Vocadlo DJ, Davies GJ, Laine R, Withers SG, Nature. 2001 Aug 23;412(6849):835-8. PMID:11518970
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