1uxt

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(New page: 200px<br /> <applet load="1uxt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uxt, resolution 2.2&Aring;" /> '''STRUCTURAL BASIS FOR...)
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==About this Structure==
==About this Structure==
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1UXT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]] with G1P, NA and NAD 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=1.2.1.9 1.2.1.9]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UXT OCA]].
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1UXT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]] with G1P, NA and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(NADP(+)) Glyceraldehyde-3-phosphate dehydrogenase (NADP(+))]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.9 1.2.1.9]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UXT OCA]].
==Reference==
==Reference==
Structural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax., Lorentzen E, Hensel R, Knura T, Ahmed H, Pohl E, J Mol Biol. 2004 Aug 13;341(3):815-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15288789 15288789]
Structural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax., Lorentzen E, Hensel R, Knura T, Ahmed H, Pohl E, J Mol Biol. 2004 Aug 13;341(3):815-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15288789 15288789]
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[[Category: Glyceraldehyde-3-phosphate dehydrogenase (NADP(+))]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermoproteus tenax]]
[[Category: Thermoproteus tenax]]
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[[Category: regulation]]
[[Category: regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:22:09 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:15:26 2007''

Revision as of 11:10, 30 October 2007


1uxt, resolution 2.2Å

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STRUCTURAL BASIS FOR ALLOSTERIC REGULATION AND SUBSTRATE SPECIFICITY OF THE NON-PHOSPHORYLATING GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE (GAPN) FROM THERMOPROTEUS TENAX

Overview

The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) of, the hyperthermophilic Archaeum Thermoproteus tenax is a member of the, superfamily of aldehyde dehydrogenases (ALDH). GAPN catalyses the, irreversible oxidation of glyceraldehyde 3-phosphate (GAP) to, 3-phosphoglycerate in the modified glycolytic pathway of this organism. In, contrast to other members of the ALDH superfamily, GAPN from T.tenax, (Tt-GAPN) is regulated by a number of intermediates and metabolites. In, the NAD-dependent oxidation of GAP, glucose 1-phosphate, fructose, 6-phosphate, AMP and ADP increase the affinity for the cosubstrate, whereas ATP, NADP, NADPH and NADH decrease it leaving, however, the, catalytic rate virtually unaltered. As we show here, the enzyme also uses, NADP as a cosubstrate, ... [(full description)]

About this Structure

1UXT is a [Single protein] structure of sequence from [Thermoproteus tenax] with G1P, NA and NAD as [ligands]. Active as [Glyceraldehyde-3-phosphate dehydrogenase (NADP(+))], with EC number [1.2.1.9]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax., Lorentzen E, Hensel R, Knura T, Ahmed H, Pohl E, J Mol Biol. 2004 Aug 13;341(3):815-28. PMID:15288789

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