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1w8s
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(New page: 200px<br /> <applet load="1w8s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w8s, resolution 1.85Å" /> '''THE MECHANISM OF TH...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1W8S 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 FBP 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=4.1.2.13 4.1.2.13]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W8S OCA]]. | + | 1W8S 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 FBP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W8S OCA]]. |
==Reference== | ==Reference== | ||
Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates., Lorentzen E, Siebers B, Hensel R, Pohl E, Biochemistry. 2005 Mar 22;44(11):4222-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15766250 15766250] | Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates., Lorentzen E, Siebers B, Hensel R, Pohl E, Biochemistry. 2005 Mar 22;44(11):4222-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15766250 15766250] | ||
| + | [[Category: Fructose-bisphosphate aldolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermoproteus tenax]] | [[Category: Thermoproteus tenax]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''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 13:58:47 2007'' |
Revision as of 11:54, 30 October 2007
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THE MECHANISM OF THE SCHIFF BASE FORMING FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE: STRUCTURAL ANALYSIS OF REACTION INTERMEDIATES
Overview
The glycolytic enzyme fructose-1,6-bisphosphate aldolase (FBPA) catalyzes, the reversible cleavage of fructose 1,6-bisphosphate to glyceraldehyde, 3-phosphate and dihydroxyacetone phosphate. Catalysis of Schiff base, forming class I FBPA relies on a number of intermediates covalently bound, to the catalytic lysine. Using active site mutants of FBPA I from, Thermoproteus tenax, we have solved the crystal structures of the enzyme, covalently bound to the carbinolamine of the substrate fructose, 1,6-bisphosphate and noncovalently bound to the cyclic form of the, substrate. The structures, determined at a resolution of 1.9 A and refined, to crystallographic R factors of 0.148 and 0.149, respectively, represent, the first view of any FBPA I in these two stages of the reaction pathway, and ... [(full description)]
About this Structure
1W8S is a [Single protein] structure of sequence from [Thermoproteus tenax] with FBP as [ligand]. Active as [Fructose-bisphosphate aldolase], with EC number [4.1.2.13]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates., Lorentzen E, Siebers B, Hensel R, Pohl E, Biochemistry. 2005 Mar 22;44(11):4222-9. PMID:15766250
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