2nuy: Difference between revisions

Revision as of 19:11, 21 February 2008

2-keto-3-deoxygluconate aldolase from Sulfolobus acidocaldarius in complex with pyruvate

OverviewOverview

Aldolases are enzymes with potential applications in biosynthesis, depending on their activity, specificity and stability. In the present study, the genomes of Sulfolobus species were screened for aldolases. Two new KDGA [2-keto-3-deoxygluconate (2-oxo-3-deoxygluconate) aldolases] from Sulfolobus acidocaldarius and Sulfolobus tokodaii were identified, overexpressed in Escherichia coli and characterized. Both enzymes were found to have biochemical properties similar to the previously characterized S. solfataricus KDGA, including the condensation of pyruvate and either D,L-glyceraldehyde or D,L-glyceraldehyde 3-phosphate. The crystal structure of S. acidocaldarius KDGA revealed the presence of a novel phosphate-binding motif that allows the formation of multiple hydrogen-bonding interactions with the acceptor substrate, and enables high activity with glyceraldehyde 3-phosphate. Activity analyses with unnatural substrates revealed that these three KDGAs readily accept aldehydes with two to four carbon atoms, and that even aldoses with five carbon atoms are accepted to some extent. Water-mediated interactions permit binding of substrates in multiple conformations in the spacious hydrophilic binding site, and correlate with the observed broad substrate specificity.

About this StructureAbout this Structure

2NUY is a Single protein structure of sequence from Sulfolobus acidocaldarius with and as ligands. Active as 2-dehydro-3-deoxy-phosphogluconate aldolase, with EC number 4.1.2.14 Full crystallographic information is available from OCA.

ReferenceReference

Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases., Wolterink-van Loo S, van Eerde A, Siemerink MA, Akerboom J, Dijkstra BW, van der Oost J, Biochem J. 2007 May 1;403(3):421-30. PMID:17176250

Page seeded by OCA on Thu Feb 21 18:11:16 2008

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OCA

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 ==Overview==
-Aldolases are enzymes with potential applications in biosynthesis, depending on their activity, specificity and stability. In the present, study, the genomes of Sulfolobus species were screened for aldolases. Two, new KDGA [2-keto-3-deoxygluconate (2-oxo-3-deoxygluconate) aldolases] from, Sulfolobus acidocaldarius and Sulfolobus tokodaii were identified, overexpressed in Escherichia coli and characterized. Both enzymes were, found to have biochemical properties similar to the previously, characterized S. solfataricus KDGA, including the condensation of pyruvate, and either D,L-glyceraldehyde or D,L-glyceraldehyde 3-phosphate. The, crystal structure of S. acidocaldarius KDGA revealed the presence of a, novel phosphate-binding motif that allows the formation of multiple, hydrogen-bonding interactions with the acceptor substrate, and enables, high activity with glyceraldehyde 3-phosphate. Activity analyses with, unnatural substrates revealed that these three KDGAs readily accept, aldehydes with two to four carbon atoms, and that even aldoses with five, carbon atoms are accepted to some extent. Water-mediated interactions, permit binding of substrates in multiple conformations in the spacious, hydrophilic binding site, and correlate with the observed broad substrate, specificity.
+Aldolases are enzymes with potential applications in biosynthesis, depending on their activity, specificity and stability. In the present study, the genomes of Sulfolobus species were screened for aldolases. Two new KDGA [2-keto-3-deoxygluconate (2-oxo-3-deoxygluconate) aldolases] from Sulfolobus acidocaldarius and Sulfolobus tokodaii were identified, overexpressed in Escherichia coli and characterized. Both enzymes were found to have biochemical properties similar to the previously characterized S. solfataricus KDGA, including the condensation of pyruvate and either D,L-glyceraldehyde or D,L-glyceraldehyde 3-phosphate. The crystal structure of S. acidocaldarius KDGA revealed the presence of a novel phosphate-binding motif that allows the formation of multiple hydrogen-bonding interactions with the acceptor substrate, and enables high activity with glyceraldehyde 3-phosphate. Activity analyses with unnatural substrates revealed that these three KDGAs readily accept aldehydes with two to four carbon atoms, and that even aldoses with five carbon atoms are accepted to some extent. Water-mediated interactions permit binding of substrates in multiple conformations in the spacious hydrophilic binding site, and correlate with the observed broad substrate specificity.
 ==About this Structure==
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 [[Category: Single protein]]
 [[Category: Sulfolobus acidocaldarius]]
-[[Category: Dijkstra, B.W.]]
+[[Category: Dijkstra, B W.]]
-[[Category: Eerde, A.van.]]
+[[Category: Eerde, A van.]]
 [[Category: MG]]
 [[Category: PYR]]
 [[Category: tim barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:59:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:16 2008''