This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1usb
From Proteopedia
(New page: 200px<br /> <applet load="1usb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1usb, resolution 2.07Å" /> '''RATIONAL DESIGN OF ...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1USB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CL, K and GSH as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1USB OCA]]. | + | 1USB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CL, K and GSH as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1USB OCA]]. |
==Reference== | ==Reference== | ||
Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1., Hederos S, Broo KS, Jakobsson E, Kleywegt GJ, Mannervik B, Baltzer L, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13163-7. Epub 2004 Aug 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15333749 15333749] | Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1., Hederos S, Broo KS, Jakobsson E, Kleywegt GJ, Mannervik B, Baltzer L, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13163-7. Epub 2004 Aug 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15333749 15333749] | ||
| + | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 23: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:55:46 2007'' |
Revision as of 11:51, 30 October 2007
|
RATIONAL DESIGN OF A NOVEL ENZYME- EFFICIENT THIOESTER HYDROLYSIS ENABLED BY THE INCORPORATION OF A SINGLE HIS RESIDUE INTO HUMAN GLUTATHIONE TRANSFERASE A1-1
Overview
A strategy for rational enzyme design is reported and illustrated by the, engineering of a protein catalyst for thiol-ester hydrolysis. Five mutants, of human glutathione (GSH; gamma-Glu-Cys-Gly) transferase A1-1 were, designed in the search for a catalyst and to provide a set of proteins, from which the reaction mechanism could be elucidated. The single mutant, A216H catalyzed the hydrolysis of the S-benzoyl ester of GSH under, turnover conditions with a k(cat)/K(M) of 156 M(-1) x min(-1), and a, catalytic proficiency of >10(7) M(-1) when compared with the first-order, rate constant of the uncatalyzed reaction. The wild-type enzyme did not, hydrolyze the substrate, and thus, the introduction of a single histidine, residue transformed the wild-type enzyme into a turnover system for, ... [(full description)]
About this Structure
1USB is a [Single protein] structure of sequence from [Homo sapiens] with CL, K and GSH as [ligands]. Active as [Glutathione transferase], with EC number [2.5.1.18]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1., Hederos S, Broo KS, Jakobsson E, Kleywegt GJ, Mannervik B, Baltzer L, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13163-7. Epub 2004 Aug 27. PMID:15333749
Page seeded by OCA on Tue Oct 30 13:55:46 2007
Categories: Glutathione transferase | Homo sapiens | Single protein | Jakobsson, E. | Kleywegt, G.J. | CL | GSH | K | Glutathione | Transferase
