1e89
From Proteopedia
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| - | [[Image:1e89.gif|left|200px]]<br /> | + | [[Image:1e89.gif|left|200px]]<br /><applet load="1e89" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1e89" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1e89, resolution 2.10Å" /> | caption="1e89, resolution 2.10Å" /> | ||
'''ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN'''<br /> | '''ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.3.2.4 Transferred entry: 3.3.2.4], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.37 4.2.1.37] | + | 1E89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.3.2.4 Transferred entry: 3.3.2.4], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.37 4.2.1.37] Known structural/functional Sites: <scene name='pdbsite=ASA:Active Site A. Catalytic Residue SER 80 Is Mutated To ALA'>ASA</scene> and <scene name='pdbsite=ASB:Active Site B. Catalytic Residue SER 80 Is Mutated To ALA'>ASB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydroxynitrile lyase]] | [[Category: hydroxynitrile lyase]] | ||
| - | ''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 15:03:54 2007'' |
Revision as of 12:54, 18 December 2007
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ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN
Overview
The structure and function of hydroxynitrile lyase from Manihot esculenta, (MeHNL) have been analyzed by X-ray crystallography and site-directed, mutagenesis. The crystal structure of the MeHNL-S80A mutant enzyme has, been refined to an R-factor of 18.0% against diffraction data to 2.1-A, resolution. The three-dimensional structure of the MeHNL-S80A-acetone, cyanohydrin complex was determined at 2.2-A resolution and refined to an, R-factor of 18.7%. Thr11 and Cys81 involved in substrate binding have been, substituted by Ala in site-directed mutagenesis. The kinetic measurements, of these mutant enzymes are presented. Combined with structural data, the, results support a mechanism for cyanogenesis in which His236 as a general, base abstracts a proton from Ser80, thereby allowing proton transfer from, the hydroxyl group of acetone cyanohydrin to Ser80. The His236 imidazolium, cation then facilitates the leaving of the nitrile group by proton, donating.
About this Structure
1E89 is a Single protein structure of sequence from Manihot esculenta. Active as Transferred entry: 3.3.2.4, with EC number 4.2.1.37 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin., Lauble H, Miehlich B, Forster S, Wajant H, Effenberger F, Protein Sci. 2001 May;10(5):1015-22. PMID:11316882
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