1ysd
From Proteopedia
(New page: 200px<br /><applet load="1ysd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ysd, resolution 1.90Å" /> '''Yeast Cytosine Deami...) |
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| - | [[Image:1ysd.gif|left|200px]]<br /><applet load="1ysd" size=" | + | [[Image:1ysd.gif|left|200px]]<br /><applet load="1ysd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ysd, resolution 1.90Å" /> | caption="1ysd, resolution 1.90Å" /> | ||
'''Yeast Cytosine Deaminase Double Mutant'''<br /> | '''Yeast Cytosine Deaminase Double Mutant'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Thermostabilizing an enzyme while maintaining its activity for industrial | + | Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10 degrees C increase in apparent melting temperature T(m) and a 30-fold increase in half-life at 50 degrees C, with no reduction in catalytic efficiency. The effects of the mutations were synergistic, giving an increase in excess of the sum of their individual effects. The redesigned enzyme induced an increased, temperature-dependent bacterial growth rate under conditions that required its activity, thereby coupling molecular and metabolic engineering. |
==About this Structure== | ==About this Structure== | ||
| - | 1YSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytosine_deaminase Cytosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.1 3.5.4.1] Full crystallographic information is available from [http:// | + | 1YSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytosine_deaminase Cytosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.1 3.5.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YSD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baker, D.]] | [[Category: Baker, D.]] | ||
| - | [[Category: Black, M | + | [[Category: Black, M E.]] |
[[Category: Korkegian, A.]] | [[Category: Korkegian, A.]] | ||
| - | [[Category: Stoddard, B | + | [[Category: Stoddard, B L.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:40 2008'' |
Revision as of 14:08, 21 February 2008
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Yeast Cytosine Deaminase Double Mutant
Overview
Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10 degrees C increase in apparent melting temperature T(m) and a 30-fold increase in half-life at 50 degrees C, with no reduction in catalytic efficiency. The effects of the mutations were synergistic, giving an increase in excess of the sum of their individual effects. The redesigned enzyme induced an increased, temperature-dependent bacterial growth rate under conditions that required its activity, thereby coupling molecular and metabolic engineering.
About this Structure
1YSD is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Cytosine deaminase, with EC number 3.5.4.1 Full crystallographic information is available from OCA.
Reference
Computational thermostabilization of an enzyme., Korkegian A, Black ME, Baker D, Stoddard BL, Science. 2005 May 6;308(5723):857-60. PMID:15879217
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