1e7m
From Proteopedia
(New page: 200px<br /> <applet load="1e7m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e7m, resolution 2.54Å" /> '''ACTIVE SITE MUTANT ...) |
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==About this Structure== | ==About this Structure== | ||
- | 1E7M is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E7M OCA]]. | + | 1E7M is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Glucose-6-phosphate_1-dehydrogenase Glucose-6-phosphate 1-dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]]. Structure known Active Site: CA1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E7M OCA]]. |
==Reference== | ==Reference== | ||
An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme., Cosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR, Biochemistry. 2000 Dec 12;39(49):15002-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106478 11106478] | An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme., Cosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR, Biochemistry. 2000 Dec 12;39(49):15002-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106478 11106478] | ||
+ | [[Category: Glucose-6-phosphate 1-dehydrogenase]] | ||
[[Category: Leuconostoc mesenteroides]] | [[Category: Leuconostoc mesenteroides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase (choh(d) - nad(p))]] | [[Category: oxidoreductase (choh(d) - nad(p))]] | ||
- | ''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 11:03:25 2007'' |
Revision as of 08:58, 30 October 2007
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ACTIVE SITE MUTANT (D177->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES
Overview
The role of Asp-177 in the His-Asp catalytic dyad of glucose 6-phosphate, dehydrogenase from Leuconostoc mesenteroides has been investigated by a, structural and functional characterization of the D177N mutant enzyme. Its, three-dimensional structure has been determined by X-ray, cryocrystallography in the presence of NAD(+) and in the presence of, glucose 6-phosphate plus NADPH. The structure of a glucose 6-phosphate, complex of a mutant (Q365C) with normal enzyme activity has also been, determined and substrate binding compared. To understand the effect of, Asp-177 on the ionization properties of the catalytic base His-240, the pH, dependence of kinetic parameters has been determined for the D177N mutant, and compared to that of the wild-type enzyme. The structures give details, of ... [(full description)]
About this Structure
1E7M is a [Single protein] structure of sequence from [Leuconostoc mesenteroides] with CA as [ligand]. Active as [Glucose-6-phosphate 1-dehydrogenase], with EC number [1.1.1.49]. Structure known Active Site: CA1. Full crystallographic information is available from [OCA].
Reference
An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme., Cosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR, Biochemistry. 2000 Dec 12;39(49):15002-11. PMID:11106478
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