1h6m: Difference between revisions

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[[Image:1h6m.gif|left|200px]]<br /><applet load="1h6m" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1h6m.gif|left|200px]]<br /><applet load="1h6m" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1h6m, resolution 1.64&Aring;" />
caption="1h6m, resolution 1.64&Aring;" />
'''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] 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].  
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 <scene name='pdbligand=NA:'>NA</scene> 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://oca.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 Tue Dec 18 16:04:03 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:47:06 2008''

Revision as of 10:47, 3 February 2008

File:1h6m.gif


1h6m, resolution 1.64Å

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COVALENT GLYCOSYL-ENZYME INTERMEDIATE OF HEN EGG WHITE LYSOZYME

OverviewOverview

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 StructureAbout this Structure

1H6M is a Single protein structure of sequence from Gallus gallus with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.

ReferenceReference

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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