2ez4
From Proteopedia
(New page: 200px<br /><applet load="2ez4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ez4, resolution 2.03Å" /> '''Pyruvate oxidase var...) |
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| - | [[Image:2ez4.gif|left|200px]]<br /><applet load="2ez4" size=" | + | [[Image:2ez4.gif|left|200px]]<br /><applet load="2ez4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ez4, resolution 2.03Å" /> | caption="2ez4, resolution 2.03Å" /> | ||
'''Pyruvate oxidase variant F479W'''<br /> | '''Pyruvate oxidase variant F479W'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Enzymes that use the cofactor thiamin diphosphate (ThDP, 1), the | + | Enzymes that use the cofactor thiamin diphosphate (ThDP, 1), the biologically active form of vitamin B(1), are involved in numerous metabolic pathways in all organisms. Although a theory of the cofactor's underlying reaction mechanism has been established over the last five decades, the three-dimensional structures of most major reaction intermediates of ThDP enzymes have remained elusive. Here, we report the X-ray structures of key intermediates in the oxidative decarboxylation of pyruvate, a central reaction in carbon metabolism catalyzed by the ThDP- and flavin-dependent enzyme pyruvate oxidase (POX)3 from Lactobacillus plantarum. The structures of 2-lactyl-ThDP (LThDP, 2) and its stable phosphonate analog, of 2-hydroxyethyl-ThDP (HEThDP, 3) enamine and of 2-acetyl-ThDP (AcThDP, 4; all shown bound to the enzyme's active site) provide profound insights into the chemical mechanisms and the stereochemical course of thiamin catalysis. These snapshots also suggest a mechanism for a phosphate-linked acyl transfer coupled to electron transfer in a radical reaction of pyruvate oxidase. |
==About this Structure== | ==About this Structure== | ||
| - | 2EZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_plantarum Lactobacillus plantarum] with MG, NA, PO4, TPP and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyruvate_oxidase Pyruvate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.3 1.2.3.3] Full crystallographic information is available from [http:// | + | 2EZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_plantarum Lactobacillus plantarum] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=TPP:'>TPP</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyruvate_oxidase Pyruvate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.3 1.2.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZ4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tpp enzyme]] | [[Category: tpp enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:59 2008'' |
Revision as of 15:16, 21 February 2008
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Pyruvate oxidase variant F479W
Overview
Enzymes that use the cofactor thiamin diphosphate (ThDP, 1), the biologically active form of vitamin B(1), are involved in numerous metabolic pathways in all organisms. Although a theory of the cofactor's underlying reaction mechanism has been established over the last five decades, the three-dimensional structures of most major reaction intermediates of ThDP enzymes have remained elusive. Here, we report the X-ray structures of key intermediates in the oxidative decarboxylation of pyruvate, a central reaction in carbon metabolism catalyzed by the ThDP- and flavin-dependent enzyme pyruvate oxidase (POX)3 from Lactobacillus plantarum. The structures of 2-lactyl-ThDP (LThDP, 2) and its stable phosphonate analog, of 2-hydroxyethyl-ThDP (HEThDP, 3) enamine and of 2-acetyl-ThDP (AcThDP, 4; all shown bound to the enzyme's active site) provide profound insights into the chemical mechanisms and the stereochemical course of thiamin catalysis. These snapshots also suggest a mechanism for a phosphate-linked acyl transfer coupled to electron transfer in a radical reaction of pyruvate oxidase.
About this Structure
2EZ4 is a Single protein structure of sequence from Lactobacillus plantarum with , , , and as ligands. Active as Pyruvate oxidase, with EC number 1.2.3.3 Full crystallographic information is available from OCA.
Reference
The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography., Wille G, Meyer D, Steinmetz A, Hinze E, Golbik R, Tittmann K, Nat Chem Biol. 2006 Jun;2(6):324-8. Epub 2006 May 7. PMID:16680160
Page seeded by OCA on Thu Feb 21 17:15:59 2008
Categories: Lactobacillus plantarum | Pyruvate oxidase | Single protein | Golbik, R. | Hinze, E. | Meyer, D. | Steinmetz, A. | Tittmann, K. | Wille, G. | FAD | MG | NA | PO4 | TPP | Tpp enzyme
