1w3n
From Proteopedia
(New page: 200px<br /> <applet load="1w3n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w3n, resolution 2.100Å" /> '''SULFOLOBUS SOLFATA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1W3N is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]] with SSH and GOL 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=4.1.2.20 4.1.2.20]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W3N OCA]]. | + | 1W3N is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]] with SSH and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/2-dehydro-3-deoxyglucarate_aldolase 2-dehydro-3-deoxyglucarate aldolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.20 4.1.2.20]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W3N OCA]]. |
==Reference== | ==Reference== | ||
The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus., Theodossis A, Walden H, Westwick EJ, Connaris H, Lamble HJ, Hough DW, Danson MJ, Taylor GL, J Biol Chem. 2004 Oct 15;279(42):43886-92. Epub 2004 Jul 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15265860 15265860] | The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus., Theodossis A, Walden H, Westwick EJ, Connaris H, Lamble HJ, Hough DW, Danson MJ, Taylor GL, J Biol Chem. 2004 Oct 15;279(42):43886-92. Epub 2004 Jul 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15265860 15265860] | ||
| + | [[Category: 2-dehydro-3-deoxyglucarate aldolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
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[[Category: d-kdg]] | [[Category: d-kdg]] | ||
| - | ''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 11:41:24 2007'' |
Revision as of 09:36, 30 October 2007
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SULFOLOBUS SOLFATARICUS 2-KETO-3-DEOXYGLUCONATE (KDG) ALDOLASE COMPLEX WITH D-KDG
Overview
The hyperthermophilic Archaea Sulfolobus solfataricus grows optimally, above 80 degrees C and metabolizes glucose by a non-phosphorylative, variant of the Entner-Doudoroff pathway. In this pathway glucose, dehydrogenase and gluconate dehydratase catalyze the oxidation of glucose, to gluconate and the subsequent dehydration of gluconate to, D-2-keto-3-deoxygluconate (KDG). KDG aldolase (KDGA) then catalyzes the, cleavage of KDG to D-glyceraldehyde and pyruvate. It has recently been, shown that all the enzymes of this pathway exhibit a catalytic promiscuity, that also enables them to be used for the metabolism of galactose. This, phenomenon, known as metabolic pathway promiscuity, depends crucially on, the ability of KDGA to cleave KDG and D-2-keto-3-deoxygalactonate (KDGal), in both cases ... [(full description)]
About this Structure
1W3N is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with SSH and GOL as [ligands]. Active as [2-dehydro-3-deoxyglucarate aldolase], with EC number [4.1.2.20]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus., Theodossis A, Walden H, Westwick EJ, Connaris H, Lamble HJ, Hough DW, Danson MJ, Taylor GL, J Biol Chem. 2004 Oct 15;279(42):43886-92. Epub 2004 Jul 20. PMID:15265860
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